| anno_start anno_end anno_text entity_type sentence section | |
| 0 33 X-ray Crystallographic Structures evidence X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17–36 β-Hairpin TITLE | |
| 39 45 Trimer oligomeric_state X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17–36 β-Hairpin TITLE | |
| 47 56 Dodecamer oligomeric_state X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17–36 β-Hairpin TITLE | |
| 62 74 Annular Pore site X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17–36 β-Hairpin TITLE | |
| 88 90 Aβ protein X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17–36 β-Hairpin TITLE | |
| 90 95 17–36 residue_range X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17–36 β-Hairpin TITLE | |
| 96 105 β-Hairpin structure_element X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17–36 β-Hairpin TITLE | |
| 16 26 structures evidence High-resolution structures of oligomers formed by the β-amyloid peptide Aβ are needed to understand the molecular basis of Alzheimer’s disease and develop therapies. ABSTRACT | |
| 30 39 oligomers oligomeric_state High-resolution structures of oligomers formed by the β-amyloid peptide Aβ are needed to understand the molecular basis of Alzheimer’s disease and develop therapies. ABSTRACT | |
| 54 71 β-amyloid peptide protein High-resolution structures of oligomers formed by the β-amyloid peptide Aβ are needed to understand the molecular basis of Alzheimer’s disease and develop therapies. ABSTRACT | |
| 72 74 Aβ protein High-resolution structures of oligomers formed by the β-amyloid peptide Aβ are needed to understand the molecular basis of Alzheimer’s disease and develop therapies. ABSTRACT | |
| 24 57 X-ray crystallographic structures evidence This paper presents the X-ray crystallographic structures of oligomers formed by a 20-residue peptide segment derived from Aβ. ABSTRACT | |
| 61 70 oligomers oligomeric_state This paper presents the X-ray crystallographic structures of oligomers formed by a 20-residue peptide segment derived from Aβ. ABSTRACT | |
| 83 109 20-residue peptide segment residue_range This paper presents the X-ray crystallographic structures of oligomers formed by a 20-residue peptide segment derived from Aβ. ABSTRACT | |
| 123 125 Aβ protein This paper presents the X-ray crystallographic structures of oligomers formed by a 20-residue peptide segment derived from Aβ. ABSTRACT | |
| 38 40 Aβ protein The development of a peptide in which Aβ17–36 is stabilized as a β-hairpin is described, and the X-ray crystallographic structures of oligomers it forms are reported. ABSTRACT | |
| 40 45 17–36 residue_range The development of a peptide in which Aβ17–36 is stabilized as a β-hairpin is described, and the X-ray crystallographic structures of oligomers it forms are reported. ABSTRACT | |
| 65 74 β-hairpin structure_element The development of a peptide in which Aβ17–36 is stabilized as a β-hairpin is described, and the X-ray crystallographic structures of oligomers it forms are reported. ABSTRACT | |
| 97 130 X-ray crystallographic structures evidence The development of a peptide in which Aβ17–36 is stabilized as a β-hairpin is described, and the X-ray crystallographic structures of oligomers it forms are reported. ABSTRACT | |
| 134 143 oligomers oligomeric_state The development of a peptide in which Aβ17–36 is stabilized as a β-hairpin is described, and the X-ray crystallographic structures of oligomers it forms are reported. ABSTRACT | |
| 56 58 Aβ protein Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 58 63 17–36 residue_range Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 77 84 hairpin structure_element Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 101 109 δ-linked protein_state Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 110 119 ornithine residue_name Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 120 124 turn structure_element Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 146 148 17 residue_number Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 153 155 36 residue_number Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 201 218 disulfide linkage ptm Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 237 239 24 residue_number Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 244 246 29 residue_number Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. ABSTRACT | |
| 30 32 33 residue_number An N-methyl group at position 33 blocks uncontrolled aggregation. ABSTRACT | |
| 12 32 readily crystallizes evidence The peptide readily crystallizes as a folded β-hairpin, which assembles hierarchically in the crystal lattice. ABSTRACT | |
| 38 44 folded protein_state The peptide readily crystallizes as a folded β-hairpin, which assembles hierarchically in the crystal lattice. ABSTRACT | |
| 45 54 β-hairpin structure_element The peptide readily crystallizes as a folded β-hairpin, which assembles hierarchically in the crystal lattice. ABSTRACT | |
| 94 109 crystal lattice evidence The peptide readily crystallizes as a folded β-hairpin, which assembles hierarchically in the crystal lattice. ABSTRACT | |
| 6 15 β-hairpin structure_element Three β-hairpin monomers assemble to form a triangular trimer, four trimers assemble in a tetrahedral arrangement to form a dodecamer, and five dodecamers pack together to form an annular pore. ABSTRACT | |
| 16 24 monomers oligomeric_state Three β-hairpin monomers assemble to form a triangular trimer, four trimers assemble in a tetrahedral arrangement to form a dodecamer, and five dodecamers pack together to form an annular pore. ABSTRACT | |
| 44 54 triangular protein_state Three β-hairpin monomers assemble to form a triangular trimer, four trimers assemble in a tetrahedral arrangement to form a dodecamer, and five dodecamers pack together to form an annular pore. ABSTRACT | |
| 55 61 trimer oligomeric_state Three β-hairpin monomers assemble to form a triangular trimer, four trimers assemble in a tetrahedral arrangement to form a dodecamer, and five dodecamers pack together to form an annular pore. ABSTRACT | |
| 68 75 trimers oligomeric_state Three β-hairpin monomers assemble to form a triangular trimer, four trimers assemble in a tetrahedral arrangement to form a dodecamer, and five dodecamers pack together to form an annular pore. ABSTRACT | |
| 124 133 dodecamer oligomeric_state Three β-hairpin monomers assemble to form a triangular trimer, four trimers assemble in a tetrahedral arrangement to form a dodecamer, and five dodecamers pack together to form an annular pore. ABSTRACT | |
| 144 154 dodecamers oligomeric_state Three β-hairpin monomers assemble to form a triangular trimer, four trimers assemble in a tetrahedral arrangement to form a dodecamer, and five dodecamers pack together to form an annular pore. ABSTRACT | |
| 180 192 annular pore site Three β-hairpin monomers assemble to form a triangular trimer, four trimers assemble in a tetrahedral arrangement to form a dodecamer, and five dodecamers pack together to form an annular pore. ABSTRACT | |
| 54 65 full-length protein_state This hierarchical assembly provides a model, in which full-length Aβ transitions from an unfolded monomer to a folded β-hairpin, which assembles to form oligomers that further pack to form an annular pore. ABSTRACT | |
| 66 68 Aβ protein This hierarchical assembly provides a model, in which full-length Aβ transitions from an unfolded monomer to a folded β-hairpin, which assembles to form oligomers that further pack to form an annular pore. ABSTRACT | |
| 89 97 unfolded protein_state This hierarchical assembly provides a model, in which full-length Aβ transitions from an unfolded monomer to a folded β-hairpin, which assembles to form oligomers that further pack to form an annular pore. ABSTRACT | |
| 98 105 monomer oligomeric_state This hierarchical assembly provides a model, in which full-length Aβ transitions from an unfolded monomer to a folded β-hairpin, which assembles to form oligomers that further pack to form an annular pore. ABSTRACT | |
| 111 117 folded protein_state This hierarchical assembly provides a model, in which full-length Aβ transitions from an unfolded monomer to a folded β-hairpin, which assembles to form oligomers that further pack to form an annular pore. ABSTRACT | |
| 118 127 β-hairpin structure_element This hierarchical assembly provides a model, in which full-length Aβ transitions from an unfolded monomer to a folded β-hairpin, which assembles to form oligomers that further pack to form an annular pore. ABSTRACT | |
| 153 162 oligomers oligomeric_state This hierarchical assembly provides a model, in which full-length Aβ transitions from an unfolded monomer to a folded β-hairpin, which assembles to form oligomers that further pack to form an annular pore. ABSTRACT | |
| 192 204 annular pore site This hierarchical assembly provides a model, in which full-length Aβ transitions from an unfolded monomer to a folded β-hairpin, which assembles to form oligomers that further pack to form an annular pore. ABSTRACT | |
| 16 26 structures evidence High-resolution structures of oligomers formed by the β-amyloid peptide Aβ are desperately needed to understand the molecular basis of Alzheimer’s disease and ultimately develop preventions or treatments. INTRO | |
| 30 39 oligomers oligomeric_state High-resolution structures of oligomers formed by the β-amyloid peptide Aβ are desperately needed to understand the molecular basis of Alzheimer’s disease and ultimately develop preventions or treatments. INTRO | |
| 54 71 β-amyloid peptide protein High-resolution structures of oligomers formed by the β-amyloid peptide Aβ are desperately needed to understand the molecular basis of Alzheimer’s disease and ultimately develop preventions or treatments. INTRO | |
| 72 74 Aβ protein High-resolution structures of oligomers formed by the β-amyloid peptide Aβ are desperately needed to understand the molecular basis of Alzheimer’s disease and ultimately develop preventions or treatments. INTRO | |
| 24 33 monomeric oligomeric_state In Alzheimer’s disease, monomeric Aβ aggregates to form soluble low molecular weight oligomers, such as dimers, trimers, tetramers, hexamers, nonamers, and dodecamers, as well as high molecular weight aggregates, such as annular protofibrils. INTRO | |
| 34 36 Aβ protein In Alzheimer’s disease, monomeric Aβ aggregates to form soluble low molecular weight oligomers, such as dimers, trimers, tetramers, hexamers, nonamers, and dodecamers, as well as high molecular weight aggregates, such as annular protofibrils. INTRO | |
| 85 94 oligomers oligomeric_state In Alzheimer’s disease, monomeric Aβ aggregates to form soluble low molecular weight oligomers, such as dimers, trimers, tetramers, hexamers, nonamers, and dodecamers, as well as high molecular weight aggregates, such as annular protofibrils. INTRO | |
| 104 110 dimers oligomeric_state In Alzheimer’s disease, monomeric Aβ aggregates to form soluble low molecular weight oligomers, such as dimers, trimers, tetramers, hexamers, nonamers, and dodecamers, as well as high molecular weight aggregates, such as annular protofibrils. INTRO | |
| 112 119 trimers oligomeric_state In Alzheimer’s disease, monomeric Aβ aggregates to form soluble low molecular weight oligomers, such as dimers, trimers, tetramers, hexamers, nonamers, and dodecamers, as well as high molecular weight aggregates, such as annular protofibrils. INTRO | |
| 121 130 tetramers oligomeric_state In Alzheimer’s disease, monomeric Aβ aggregates to form soluble low molecular weight oligomers, such as dimers, trimers, tetramers, hexamers, nonamers, and dodecamers, as well as high molecular weight aggregates, such as annular protofibrils. INTRO | |
| 132 140 hexamers oligomeric_state In Alzheimer’s disease, monomeric Aβ aggregates to form soluble low molecular weight oligomers, such as dimers, trimers, tetramers, hexamers, nonamers, and dodecamers, as well as high molecular weight aggregates, such as annular protofibrils. INTRO | |
| 142 150 nonamers oligomeric_state In Alzheimer’s disease, monomeric Aβ aggregates to form soluble low molecular weight oligomers, such as dimers, trimers, tetramers, hexamers, nonamers, and dodecamers, as well as high molecular weight aggregates, such as annular protofibrils. INTRO | |
| 156 166 dodecamers oligomeric_state In Alzheimer’s disease, monomeric Aβ aggregates to form soluble low molecular weight oligomers, such as dimers, trimers, tetramers, hexamers, nonamers, and dodecamers, as well as high molecular weight aggregates, such as annular protofibrils. INTRO | |
| 221 241 annular protofibrils complex_assembly In Alzheimer’s disease, monomeric Aβ aggregates to form soluble low molecular weight oligomers, such as dimers, trimers, tetramers, hexamers, nonamers, and dodecamers, as well as high molecular weight aggregates, such as annular protofibrils. INTRO | |
| 38 40 Aβ protein Over the last two decades the role of Aβ oligomers in the pathophysiology of Alzheimer’s disease has begun to unfold. INTRO | |
| 41 50 oligomers oligomeric_state Over the last two decades the role of Aβ oligomers in the pathophysiology of Alzheimer’s disease has begun to unfold. INTRO | |
| 0 5 Mouse taxonomy_domain Mouse models for Alzheimer’s disease have helped shape our current understanding about the Aβ oligomerization that precedes neurodegeneration. INTRO | |
| 91 93 Aβ protein Mouse models for Alzheimer’s disease have helped shape our current understanding about the Aβ oligomerization that precedes neurodegeneration. INTRO | |
| 0 2 Aβ protein Aβ isolated from the brains of young plaque-free Tg2576 mice forms a mixture of low molecular weight oligomers. INTRO | |
| 56 60 mice taxonomy_domain Aβ isolated from the brains of young plaque-free Tg2576 mice forms a mixture of low molecular weight oligomers. INTRO | |
| 101 110 oligomers oligomeric_state Aβ isolated from the brains of young plaque-free Tg2576 mice forms a mixture of low molecular weight oligomers. INTRO | |
| 17 25 oligomer oligomeric_state A 56 kDa soluble oligomer identified by SDS-PAGE was found to be especially important within this mixture. INTRO | |
| 40 48 SDS-PAGE experimental_method A 56 kDa soluble oligomer identified by SDS-PAGE was found to be especially important within this mixture. INTRO | |
| 5 13 oligomer oligomeric_state This oligomer was termed Aβ*56 and appears to be a dodecamer of Aβ. INTRO | |
| 25 30 Aβ*56 complex_assembly This oligomer was termed Aβ*56 and appears to be a dodecamer of Aβ. INTRO | |
| 51 60 dodecamer oligomeric_state This oligomer was termed Aβ*56 and appears to be a dodecamer of Aβ. INTRO | |
| 64 66 Aβ protein This oligomer was termed Aβ*56 and appears to be a dodecamer of Aβ. INTRO | |
| 9 14 Aβ*56 complex_assembly Purified Aβ*56 injected intercranially into healthy rats was found to impair memory, providing evidence that this Aβ oligomer may cause memory loss in Alzheimer’s disease. INTRO | |
| 15 38 injected intercranially experimental_method Purified Aβ*56 injected intercranially into healthy rats was found to impair memory, providing evidence that this Aβ oligomer may cause memory loss in Alzheimer’s disease. INTRO | |
| 52 56 rats taxonomy_domain Purified Aβ*56 injected intercranially into healthy rats was found to impair memory, providing evidence that this Aβ oligomer may cause memory loss in Alzheimer’s disease. INTRO | |
| 114 116 Aβ protein Purified Aβ*56 injected intercranially into healthy rats was found to impair memory, providing evidence that this Aβ oligomer may cause memory loss in Alzheimer’s disease. INTRO | |
| 117 125 oligomer oligomeric_state Purified Aβ*56 injected intercranially into healthy rats was found to impair memory, providing evidence that this Aβ oligomer may cause memory loss in Alzheimer’s disease. INTRO | |
| 8 17 oligomers oligomeric_state Smaller oligomers with molecular weights consistent with trimers, hexamers, and nonamers were also identified within the mixture of low molecular weight oligomers. INTRO | |
| 57 64 trimers oligomeric_state Smaller oligomers with molecular weights consistent with trimers, hexamers, and nonamers were also identified within the mixture of low molecular weight oligomers. INTRO | |
| 66 74 hexamers oligomeric_state Smaller oligomers with molecular weights consistent with trimers, hexamers, and nonamers were also identified within the mixture of low molecular weight oligomers. INTRO | |
| 80 88 nonamers oligomeric_state Smaller oligomers with molecular weights consistent with trimers, hexamers, and nonamers were also identified within the mixture of low molecular weight oligomers. INTRO | |
| 153 162 oligomers oligomeric_state Smaller oligomers with molecular weights consistent with trimers, hexamers, and nonamers were also identified within the mixture of low molecular weight oligomers. INTRO | |
| 49 58 oligomers oligomeric_state Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 64 85 hexafluoroisopropanol chemical Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 131 141 dodecamers oligomeric_state Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 143 151 nonamers oligomeric_state Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 157 165 hexamers oligomeric_state Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 171 178 trimers oligomeric_state Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 183 191 monomers oligomeric_state Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 209 216 trimers oligomeric_state Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 250 260 dodecamers oligomeric_state Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 262 270 nonamers oligomeric_state Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 276 284 hexamers oligomeric_state Treatment of the mixture of low molecular weight oligomers with hexafluoroisopropanol resulted in the dissociation of the putative dodecamers, nonamers, and hexamers into trimers and monomers, suggesting that trimers may be the building block of the dodecamers, nonamers, and hexamers. INTRO | |
| 10 12 Aβ protein Recently, Aβ trimers and Aβ*56 were identified in the brains of cognitively normal humans and were found to increase with age. INTRO | |
| 13 20 trimers oligomeric_state Recently, Aβ trimers and Aβ*56 were identified in the brains of cognitively normal humans and were found to increase with age. INTRO | |
| 25 30 Aβ*56 complex_assembly Recently, Aβ trimers and Aβ*56 were identified in the brains of cognitively normal humans and were found to increase with age. INTRO | |
| 83 89 humans species Recently, Aβ trimers and Aβ*56 were identified in the brains of cognitively normal humans and were found to increase with age. INTRO | |
| 16 25 oligomers oligomeric_state A type of large oligomers called annular protofibrils (APFs) have also been observed in the brains of transgenic mice and isolated from the brains of Alzheimer’s patients. INTRO | |
| 33 53 annular protofibrils complex_assembly A type of large oligomers called annular protofibrils (APFs) have also been observed in the brains of transgenic mice and isolated from the brains of Alzheimer’s patients. INTRO | |
| 55 59 APFs complex_assembly A type of large oligomers called annular protofibrils (APFs) have also been observed in the brains of transgenic mice and isolated from the brains of Alzheimer’s patients. INTRO | |
| 113 117 mice taxonomy_domain A type of large oligomers called annular protofibrils (APFs) have also been observed in the brains of transgenic mice and isolated from the brains of Alzheimer’s patients. INTRO | |
| 0 4 APFs complex_assembly APFs were first discovered in vitro using chemically synthesized Aβ that aggregated into porelike structures that could be observed by atomic force microscopy (AFM) and transmission electron microscopy (TEM). INTRO | |
| 42 64 chemically synthesized protein_state APFs were first discovered in vitro using chemically synthesized Aβ that aggregated into porelike structures that could be observed by atomic force microscopy (AFM) and transmission electron microscopy (TEM). INTRO | |
| 65 67 Aβ protein APFs were first discovered in vitro using chemically synthesized Aβ that aggregated into porelike structures that could be observed by atomic force microscopy (AFM) and transmission electron microscopy (TEM). INTRO | |
| 89 108 porelike structures structure_element APFs were first discovered in vitro using chemically synthesized Aβ that aggregated into porelike structures that could be observed by atomic force microscopy (AFM) and transmission electron microscopy (TEM). INTRO | |
| 135 158 atomic force microscopy experimental_method APFs were first discovered in vitro using chemically synthesized Aβ that aggregated into porelike structures that could be observed by atomic force microscopy (AFM) and transmission electron microscopy (TEM). INTRO | |
| 160 163 AFM experimental_method APFs were first discovered in vitro using chemically synthesized Aβ that aggregated into porelike structures that could be observed by atomic force microscopy (AFM) and transmission electron microscopy (TEM). INTRO | |
| 169 201 transmission electron microscopy experimental_method APFs were first discovered in vitro using chemically synthesized Aβ that aggregated into porelike structures that could be observed by atomic force microscopy (AFM) and transmission electron microscopy (TEM). INTRO | |
| 203 206 TEM experimental_method APFs were first discovered in vitro using chemically synthesized Aβ that aggregated into porelike structures that could be observed by atomic force microscopy (AFM) and transmission electron microscopy (TEM). INTRO | |
| 13 17 APFs complex_assembly The sizes of APFs prepared in vitro vary among different studies. INTRO | |
| 24 28 APFs complex_assembly Lashuel et al. observed APFs with an outer diameter that ranged from 7–10 nm and an inner diameter that ranged from 1.5–2 nm, consistent with molecular weights of 150–250 kDa. INTRO | |
| 22 26 APFs complex_assembly Quist et al. observed APFs with an outer diameter of 16 nm embedded in a lipid bilayer. INTRO | |
| 22 26 APFs complex_assembly Kayed et al. observed APFs with an outer diameter that ranged from 8–25 nm, which were composed of small spherical Aβ oligomers, 3–5 nm in diameter. INTRO | |
| 99 114 small spherical protein_state Kayed et al. observed APFs with an outer diameter that ranged from 8–25 nm, which were composed of small spherical Aβ oligomers, 3–5 nm in diameter. INTRO | |
| 115 117 Aβ protein Kayed et al. observed APFs with an outer diameter that ranged from 8–25 nm, which were composed of small spherical Aβ oligomers, 3–5 nm in diameter. INTRO | |
| 118 127 oligomers oligomeric_state Kayed et al. observed APFs with an outer diameter that ranged from 8–25 nm, which were composed of small spherical Aβ oligomers, 3–5 nm in diameter. INTRO | |
| 13 17 APFs complex_assembly Although the APFs in these studies differ in size, they share a similar annular morphology and appear to be composed of smaller oligomers. INTRO | |
| 128 137 oligomers oligomeric_state Although the APFs in these studies differ in size, they share a similar annular morphology and appear to be composed of smaller oligomers. INTRO | |
| 0 4 APFs complex_assembly APFs have also been observed in the brains of APP23 transgenic mice by immunofluorescence with an anti-APF antibody and were found to accumulate in neuronal processes and synapses. INTRO | |
| 63 67 mice taxonomy_domain APFs have also been observed in the brains of APP23 transgenic mice by immunofluorescence with an anti-APF antibody and were found to accumulate in neuronal processes and synapses. INTRO | |
| 71 89 immunofluorescence experimental_method APFs have also been observed in the brains of APP23 transgenic mice by immunofluorescence with an anti-APF antibody and were found to accumulate in neuronal processes and synapses. INTRO | |
| 103 106 APF complex_assembly APFs have also been observed in the brains of APP23 transgenic mice by immunofluorescence with an anti-APF antibody and were found to accumulate in neuronal processes and synapses. INTRO | |
| 23 27 APFs complex_assembly In a subsequent study, APFs were isolated from the brains of Alzheimer’s patients by immunoprecipitation with an anti-APF antibody. INTRO | |
| 85 104 immunoprecipitation experimental_method In a subsequent study, APFs were isolated from the brains of Alzheimer’s patients by immunoprecipitation with an anti-APF antibody. INTRO | |
| 118 121 APF complex_assembly In a subsequent study, APFs were isolated from the brains of Alzheimer’s patients by immunoprecipitation with an anti-APF antibody. INTRO | |
| 6 10 APFs complex_assembly These APFs had an outer diameter that ranged from 11–14 nm and an inner diameter that ranged from 2.5–4 nm. INTRO | |
| 0 6 Dimers oligomeric_state Dimers of Aβ have also been isolated from the brains of Alzheimer’s patients.− Aβ dimers inhibit long-term potentiation in mice and promote hyperphosphorylation of the microtubule-associated protein tau, leading to neuritic damage. INTRO | |
| 10 12 Aβ protein Dimers of Aβ have also been isolated from the brains of Alzheimer’s patients.− Aβ dimers inhibit long-term potentiation in mice and promote hyperphosphorylation of the microtubule-associated protein tau, leading to neuritic damage. INTRO | |
| 79 81 Aβ protein Dimers of Aβ have also been isolated from the brains of Alzheimer’s patients.− Aβ dimers inhibit long-term potentiation in mice and promote hyperphosphorylation of the microtubule-associated protein tau, leading to neuritic damage. INTRO | |
| 82 88 dimers oligomeric_state Dimers of Aβ have also been isolated from the brains of Alzheimer’s patients.− Aβ dimers inhibit long-term potentiation in mice and promote hyperphosphorylation of the microtubule-associated protein tau, leading to neuritic damage. INTRO | |
| 123 127 mice taxonomy_domain Dimers of Aβ have also been isolated from the brains of Alzheimer’s patients.− Aβ dimers inhibit long-term potentiation in mice and promote hyperphosphorylation of the microtubule-associated protein tau, leading to neuritic damage. INTRO | |
| 140 160 hyperphosphorylation ptm Dimers of Aβ have also been isolated from the brains of Alzheimer’s patients.− Aβ dimers inhibit long-term potentiation in mice and promote hyperphosphorylation of the microtubule-associated protein tau, leading to neuritic damage. INTRO | |
| 168 202 microtubule-associated protein tau protein Dimers of Aβ have also been isolated from the brains of Alzheimer’s patients.− Aβ dimers inhibit long-term potentiation in mice and promote hyperphosphorylation of the microtubule-associated protein tau, leading to neuritic damage. INTRO | |
| 0 2 Aβ protein Aβ dimers have only been isolated from human or transgenic mouse brains that contain the pathognomonic fibrillar Aβ plaques associated with Alzheimer’s disease. INTRO | |
| 3 9 dimers oligomeric_state Aβ dimers have only been isolated from human or transgenic mouse brains that contain the pathognomonic fibrillar Aβ plaques associated with Alzheimer’s disease. INTRO | |
| 39 44 human species Aβ dimers have only been isolated from human or transgenic mouse brains that contain the pathognomonic fibrillar Aβ plaques associated with Alzheimer’s disease. INTRO | |
| 59 64 mouse taxonomy_domain Aβ dimers have only been isolated from human or transgenic mouse brains that contain the pathognomonic fibrillar Aβ plaques associated with Alzheimer’s disease. INTRO | |
| 103 112 fibrillar protein_state Aβ dimers have only been isolated from human or transgenic mouse brains that contain the pathognomonic fibrillar Aβ plaques associated with Alzheimer’s disease. INTRO | |
| 113 115 Aβ protein Aβ dimers have only been isolated from human or transgenic mouse brains that contain the pathognomonic fibrillar Aβ plaques associated with Alzheimer’s disease. INTRO | |
| 36 38 Aβ protein Furthermore, the endogenous rise of Aβ dimers in the brains of Tg2576 and J20 transgenic mice coincides with the deposition of Aβ plaques. INTRO | |
| 39 45 dimers oligomeric_state Furthermore, the endogenous rise of Aβ dimers in the brains of Tg2576 and J20 transgenic mice coincides with the deposition of Aβ plaques. INTRO | |
| 89 93 mice taxonomy_domain Furthermore, the endogenous rise of Aβ dimers in the brains of Tg2576 and J20 transgenic mice coincides with the deposition of Aβ plaques. INTRO | |
| 127 129 Aβ protein Furthermore, the endogenous rise of Aβ dimers in the brains of Tg2576 and J20 transgenic mice coincides with the deposition of Aβ plaques. INTRO | |
| 36 38 Aβ protein These observations suggest that the Aβ trimers, hexamers, dodecamers, and related assemblies may be associated with presymptomatic neurodegeneration, while Aβ dimers are more closely associated with fibril formation and plaque deposition during symptomatic Alzheimer’s disease.− INTRO | |
| 39 46 trimers oligomeric_state These observations suggest that the Aβ trimers, hexamers, dodecamers, and related assemblies may be associated with presymptomatic neurodegeneration, while Aβ dimers are more closely associated with fibril formation and plaque deposition during symptomatic Alzheimer’s disease.− INTRO | |
| 48 56 hexamers oligomeric_state These observations suggest that the Aβ trimers, hexamers, dodecamers, and related assemblies may be associated with presymptomatic neurodegeneration, while Aβ dimers are more closely associated with fibril formation and plaque deposition during symptomatic Alzheimer’s disease.− INTRO | |
| 58 68 dodecamers oligomeric_state These observations suggest that the Aβ trimers, hexamers, dodecamers, and related assemblies may be associated with presymptomatic neurodegeneration, while Aβ dimers are more closely associated with fibril formation and plaque deposition during symptomatic Alzheimer’s disease.− INTRO | |
| 156 158 Aβ protein These observations suggest that the Aβ trimers, hexamers, dodecamers, and related assemblies may be associated with presymptomatic neurodegeneration, while Aβ dimers are more closely associated with fibril formation and plaque deposition during symptomatic Alzheimer’s disease.− INTRO | |
| 159 165 dimers oligomeric_state These observations suggest that the Aβ trimers, hexamers, dodecamers, and related assemblies may be associated with presymptomatic neurodegeneration, while Aβ dimers are more closely associated with fibril formation and plaque deposition during symptomatic Alzheimer’s disease.− INTRO | |
| 45 47 Aβ protein The approach of isolating and characterizing Aβ oligomers has not provided any high-resolution structures of Aβ oligomers. INTRO | |
| 48 57 oligomers oligomeric_state The approach of isolating and characterizing Aβ oligomers has not provided any high-resolution structures of Aβ oligomers. INTRO | |
| 95 105 structures evidence The approach of isolating and characterizing Aβ oligomers has not provided any high-resolution structures of Aβ oligomers. INTRO | |
| 109 111 Aβ protein The approach of isolating and characterizing Aβ oligomers has not provided any high-resolution structures of Aβ oligomers. INTRO | |
| 112 121 oligomers oligomeric_state The approach of isolating and characterizing Aβ oligomers has not provided any high-resolution structures of Aβ oligomers. INTRO | |
| 19 27 SDS-PAGE experimental_method Techniques such as SDS-PAGE, TEM, and AFM have only provided information about the molecular weights, sizes, morphologies, and stoichiometry of Aβ oligomers. INTRO | |
| 29 32 TEM experimental_method Techniques such as SDS-PAGE, TEM, and AFM have only provided information about the molecular weights, sizes, morphologies, and stoichiometry of Aβ oligomers. INTRO | |
| 38 41 AFM experimental_method Techniques such as SDS-PAGE, TEM, and AFM have only provided information about the molecular weights, sizes, morphologies, and stoichiometry of Aβ oligomers. INTRO | |
| 144 146 Aβ protein Techniques such as SDS-PAGE, TEM, and AFM have only provided information about the molecular weights, sizes, morphologies, and stoichiometry of Aβ oligomers. INTRO | |
| 147 156 oligomers oligomeric_state Techniques such as SDS-PAGE, TEM, and AFM have only provided information about the molecular weights, sizes, morphologies, and stoichiometry of Aβ oligomers. INTRO | |
| 16 34 structural studies experimental_method High-resolution structural studies of Aβ have primarily focused on Aβ fibrils and Aβ monomers. INTRO | |
| 38 40 Aβ protein High-resolution structural studies of Aβ have primarily focused on Aβ fibrils and Aβ monomers. INTRO | |
| 67 69 Aβ protein High-resolution structural studies of Aβ have primarily focused on Aβ fibrils and Aβ monomers. INTRO | |
| 70 77 fibrils oligomeric_state High-resolution structural studies of Aβ have primarily focused on Aβ fibrils and Aβ monomers. INTRO | |
| 82 84 Aβ protein High-resolution structural studies of Aβ have primarily focused on Aβ fibrils and Aβ monomers. INTRO | |
| 85 93 monomers oligomeric_state High-resolution structural studies of Aβ have primarily focused on Aβ fibrils and Aβ monomers. INTRO | |
| 0 28 Solid-state NMR spectroscopy experimental_method Solid-state NMR spectroscopy studies of Aβ fibrils revealed that Aβ fibrils are generally composed of extended networks of in-register parallel β-sheets.− X-ray crystallographic studies using fragments of Aβ have provided additional information about how Aβ fibrils pack. INTRO | |
| 40 42 Aβ protein Solid-state NMR spectroscopy studies of Aβ fibrils revealed that Aβ fibrils are generally composed of extended networks of in-register parallel β-sheets.− X-ray crystallographic studies using fragments of Aβ have provided additional information about how Aβ fibrils pack. INTRO | |
| 43 50 fibrils oligomeric_state Solid-state NMR spectroscopy studies of Aβ fibrils revealed that Aβ fibrils are generally composed of extended networks of in-register parallel β-sheets.− X-ray crystallographic studies using fragments of Aβ have provided additional information about how Aβ fibrils pack. INTRO | |
| 65 67 Aβ protein Solid-state NMR spectroscopy studies of Aβ fibrils revealed that Aβ fibrils are generally composed of extended networks of in-register parallel β-sheets.− X-ray crystallographic studies using fragments of Aβ have provided additional information about how Aβ fibrils pack. INTRO | |
| 68 75 fibrils oligomeric_state Solid-state NMR spectroscopy studies of Aβ fibrils revealed that Aβ fibrils are generally composed of extended networks of in-register parallel β-sheets.− X-ray crystallographic studies using fragments of Aβ have provided additional information about how Aβ fibrils pack. INTRO | |
| 123 152 in-register parallel β-sheets structure_element Solid-state NMR spectroscopy studies of Aβ fibrils revealed that Aβ fibrils are generally composed of extended networks of in-register parallel β-sheets.− X-ray crystallographic studies using fragments of Aβ have provided additional information about how Aβ fibrils pack. INTRO | |
| 155 185 X-ray crystallographic studies experimental_method Solid-state NMR spectroscopy studies of Aβ fibrils revealed that Aβ fibrils are generally composed of extended networks of in-register parallel β-sheets.− X-ray crystallographic studies using fragments of Aβ have provided additional information about how Aβ fibrils pack. INTRO | |
| 205 207 Aβ protein Solid-state NMR spectroscopy studies of Aβ fibrils revealed that Aβ fibrils are generally composed of extended networks of in-register parallel β-sheets.− X-ray crystallographic studies using fragments of Aβ have provided additional information about how Aβ fibrils pack. INTRO | |
| 255 257 Aβ protein Solid-state NMR spectroscopy studies of Aβ fibrils revealed that Aβ fibrils are generally composed of extended networks of in-register parallel β-sheets.− X-ray crystallographic studies using fragments of Aβ have provided additional information about how Aβ fibrils pack. INTRO | |
| 258 265 fibrils oligomeric_state Solid-state NMR spectroscopy studies of Aβ fibrils revealed that Aβ fibrils are generally composed of extended networks of in-register parallel β-sheets.− X-ray crystallographic studies using fragments of Aβ have provided additional information about how Aβ fibrils pack. INTRO | |
| 0 18 Solution-phase NMR experimental_method Solution-phase NMR and solid-state NMR have been used to study the structures of the Aβ monomers within oligomeric assemblies.− A major finding from these studies is that oligomeric assemblies of Aβ are primarily composed of antiparallel β-sheets. INTRO | |
| 23 38 solid-state NMR experimental_method Solution-phase NMR and solid-state NMR have been used to study the structures of the Aβ monomers within oligomeric assemblies.− A major finding from these studies is that oligomeric assemblies of Aβ are primarily composed of antiparallel β-sheets. INTRO | |
| 67 77 structures evidence Solution-phase NMR and solid-state NMR have been used to study the structures of the Aβ monomers within oligomeric assemblies.− A major finding from these studies is that oligomeric assemblies of Aβ are primarily composed of antiparallel β-sheets. INTRO | |
| 85 87 Aβ protein Solution-phase NMR and solid-state NMR have been used to study the structures of the Aβ monomers within oligomeric assemblies.− A major finding from these studies is that oligomeric assemblies of Aβ are primarily composed of antiparallel β-sheets. INTRO | |
| 88 96 monomers oligomeric_state Solution-phase NMR and solid-state NMR have been used to study the structures of the Aβ monomers within oligomeric assemblies.− A major finding from these studies is that oligomeric assemblies of Aβ are primarily composed of antiparallel β-sheets. INTRO | |
| 196 198 Aβ protein Solution-phase NMR and solid-state NMR have been used to study the structures of the Aβ monomers within oligomeric assemblies.− A major finding from these studies is that oligomeric assemblies of Aβ are primarily composed of antiparallel β-sheets. INTRO | |
| 225 246 antiparallel β-sheets structure_element Solution-phase NMR and solid-state NMR have been used to study the structures of the Aβ monomers within oligomeric assemblies.− A major finding from these studies is that oligomeric assemblies of Aβ are primarily composed of antiparallel β-sheets. INTRO | |
| 40 47 monomer oligomeric_state Many of these studies have reported the monomer subunit as adopting a β-hairpin conformation, in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. INTRO | |
| 48 55 subunit structure_element Many of these studies have reported the monomer subunit as adopting a β-hairpin conformation, in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. INTRO | |
| 70 79 β-hairpin structure_element Many of these studies have reported the monomer subunit as adopting a β-hairpin conformation, in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. INTRO | |
| 119 126 central structure_element Many of these studies have reported the monomer subunit as adopting a β-hairpin conformation, in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. INTRO | |
| 131 149 C-terminal regions structure_element Many of these studies have reported the monomer subunit as adopting a β-hairpin conformation, in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. INTRO | |
| 158 178 antiparallel β-sheet structure_element Many of these studies have reported the monomer subunit as adopting a β-hairpin conformation, in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. INTRO | |
| 35 38 NMR experimental_method In 2008, Hoyer et al. reported the NMR structure of an Aβ monomer bound to an artificial binding protein called an affibody (PDB 2OTK). INTRO | |
| 39 48 structure evidence In 2008, Hoyer et al. reported the NMR structure of an Aβ monomer bound to an artificial binding protein called an affibody (PDB 2OTK). INTRO | |
| 55 57 Aβ protein In 2008, Hoyer et al. reported the NMR structure of an Aβ monomer bound to an artificial binding protein called an affibody (PDB 2OTK). INTRO | |
| 58 65 monomer oligomeric_state In 2008, Hoyer et al. reported the NMR structure of an Aβ monomer bound to an artificial binding protein called an affibody (PDB 2OTK). INTRO | |
| 66 74 bound to protein_state In 2008, Hoyer et al. reported the NMR structure of an Aβ monomer bound to an artificial binding protein called an affibody (PDB 2OTK). INTRO | |
| 78 104 artificial binding protein chemical In 2008, Hoyer et al. reported the NMR structure of an Aβ monomer bound to an artificial binding protein called an affibody (PDB 2OTK). INTRO | |
| 115 123 affibody chemical In 2008, Hoyer et al. reported the NMR structure of an Aβ monomer bound to an artificial binding protein called an affibody (PDB 2OTK). INTRO | |
| 4 13 structure evidence The structure revealed that monomeric Aβ forms a β-hairpin when bound to the affibody. INTRO | |
| 28 37 monomeric oligomeric_state The structure revealed that monomeric Aβ forms a β-hairpin when bound to the affibody. INTRO | |
| 38 40 Aβ protein The structure revealed that monomeric Aβ forms a β-hairpin when bound to the affibody. INTRO | |
| 49 58 β-hairpin structure_element The structure revealed that monomeric Aβ forms a β-hairpin when bound to the affibody. INTRO | |
| 64 72 bound to protein_state The structure revealed that monomeric Aβ forms a β-hairpin when bound to the affibody. INTRO | |
| 77 85 affibody chemical The structure revealed that monomeric Aβ forms a β-hairpin when bound to the affibody. INTRO | |
| 5 7 Aβ protein This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 8 17 β-hairpin structure_element This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 39 44 17–37 residue_range This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 62 71 β-strands structure_element This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 83 85 Aβ protein This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 85 90 17–24 residue_range This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 95 97 Aβ protein This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 97 102 30–37 residue_range This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 119 121 Aβ protein This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 121 126 25–29 residue_range This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 127 131 loop structure_element This Aβ β-hairpin encompasses residues 17–37 and contains two β-strands comprising Aβ17–24 and Aβ30–37 connected by an Aβ25–29 loop. INTRO | |
| 13 15 Aβ protein Sequestering Aβ within the affibody prevents its fibrilization and reduces its neurotoxicity, providing evidence that the β-hairpin structure may contribute to the ability of Aβ to form neurotoxic oligomers. INTRO | |
| 27 35 affibody chemical Sequestering Aβ within the affibody prevents its fibrilization and reduces its neurotoxicity, providing evidence that the β-hairpin structure may contribute to the ability of Aβ to form neurotoxic oligomers. INTRO | |
| 122 131 β-hairpin structure_element Sequestering Aβ within the affibody prevents its fibrilization and reduces its neurotoxicity, providing evidence that the β-hairpin structure may contribute to the ability of Aβ to form neurotoxic oligomers. INTRO | |
| 175 177 Aβ protein Sequestering Aβ within the affibody prevents its fibrilization and reduces its neurotoxicity, providing evidence that the β-hairpin structure may contribute to the ability of Aβ to form neurotoxic oligomers. INTRO | |
| 197 206 oligomers oligomeric_state Sequestering Aβ within the affibody prevents its fibrilization and reduces its neurotoxicity, providing evidence that the β-hairpin structure may contribute to the ability of Aβ to form neurotoxic oligomers. INTRO | |
| 48 50 Aβ protein In a related study, Sandberg et al. constrained Aβ in a β-hairpin conformation by mutating residues A21 and A30 to cysteine and forming an intramolecular disulfide bond. INTRO | |
| 56 65 β-hairpin structure_element In a related study, Sandberg et al. constrained Aβ in a β-hairpin conformation by mutating residues A21 and A30 to cysteine and forming an intramolecular disulfide bond. INTRO | |
| 82 90 mutating experimental_method In a related study, Sandberg et al. constrained Aβ in a β-hairpin conformation by mutating residues A21 and A30 to cysteine and forming an intramolecular disulfide bond. INTRO | |
| 100 103 A21 residue_name_number In a related study, Sandberg et al. constrained Aβ in a β-hairpin conformation by mutating residues A21 and A30 to cysteine and forming an intramolecular disulfide bond. INTRO | |
| 108 111 A30 residue_name_number In a related study, Sandberg et al. constrained Aβ in a β-hairpin conformation by mutating residues A21 and A30 to cysteine and forming an intramolecular disulfide bond. INTRO | |
| 115 123 cysteine residue_name In a related study, Sandberg et al. constrained Aβ in a β-hairpin conformation by mutating residues A21 and A30 to cysteine and forming an intramolecular disulfide bond. INTRO | |
| 154 168 disulfide bond ptm In a related study, Sandberg et al. constrained Aβ in a β-hairpin conformation by mutating residues A21 and A30 to cysteine and forming an intramolecular disulfide bond. INTRO | |
| 8 10 Aβ protein Locking Aβ into a β-hairpin structure resulted in the formation Aβ oligomers, which were observed by size exclusion chromatography (SEC) and SDS-PAGE. INTRO | |
| 18 27 β-hairpin structure_element Locking Aβ into a β-hairpin structure resulted in the formation Aβ oligomers, which were observed by size exclusion chromatography (SEC) and SDS-PAGE. INTRO | |
| 64 66 Aβ protein Locking Aβ into a β-hairpin structure resulted in the formation Aβ oligomers, which were observed by size exclusion chromatography (SEC) and SDS-PAGE. INTRO | |
| 67 76 oligomers oligomeric_state Locking Aβ into a β-hairpin structure resulted in the formation Aβ oligomers, which were observed by size exclusion chromatography (SEC) and SDS-PAGE. INTRO | |
| 101 130 size exclusion chromatography experimental_method Locking Aβ into a β-hairpin structure resulted in the formation Aβ oligomers, which were observed by size exclusion chromatography (SEC) and SDS-PAGE. INTRO | |
| 132 135 SEC experimental_method Locking Aβ into a β-hairpin structure resulted in the formation Aβ oligomers, which were observed by size exclusion chromatography (SEC) and SDS-PAGE. INTRO | |
| 141 149 SDS-PAGE experimental_method Locking Aβ into a β-hairpin structure resulted in the formation Aβ oligomers, which were observed by size exclusion chromatography (SEC) and SDS-PAGE. INTRO | |
| 4 13 oligomers oligomeric_state The oligomers with a molecular weight of ∼100 kDa that were isolated by SEC were toxic toward neuronally derived SH-SY5Y cells. INTRO | |
| 72 75 SEC experimental_method The oligomers with a molecular weight of ∼100 kDa that were isolated by SEC were toxic toward neuronally derived SH-SY5Y cells. INTRO | |
| 45 54 β-hairpin structure_element This study provides evidence for the role of β-hairpin structure in Aβ oligomerization and neurotoxicity. INTRO | |
| 68 70 Aβ protein This study provides evidence for the role of β-hairpin structure in Aβ oligomerization and neurotoxicity. INTRO | |
| 18 27 β-hairpin structure_element Inspired by these β-hairpin structures, our laboratory developed a macrocyclic β-sheet peptide derived from Aβ17–36 designed to mimic an Aβ β-hairpin and reported its X-ray crystallographic structure. INTRO | |
| 28 38 structures evidence Inspired by these β-hairpin structures, our laboratory developed a macrocyclic β-sheet peptide derived from Aβ17–36 designed to mimic an Aβ β-hairpin and reported its X-ray crystallographic structure. INTRO | |
| 79 86 β-sheet structure_element Inspired by these β-hairpin structures, our laboratory developed a macrocyclic β-sheet peptide derived from Aβ17–36 designed to mimic an Aβ β-hairpin and reported its X-ray crystallographic structure. INTRO | |
| 108 110 Aβ protein Inspired by these β-hairpin structures, our laboratory developed a macrocyclic β-sheet peptide derived from Aβ17–36 designed to mimic an Aβ β-hairpin and reported its X-ray crystallographic structure. INTRO | |
| 110 115 17–36 residue_range Inspired by these β-hairpin structures, our laboratory developed a macrocyclic β-sheet peptide derived from Aβ17–36 designed to mimic an Aβ β-hairpin and reported its X-ray crystallographic structure. INTRO | |
| 137 139 Aβ protein Inspired by these β-hairpin structures, our laboratory developed a macrocyclic β-sheet peptide derived from Aβ17–36 designed to mimic an Aβ β-hairpin and reported its X-ray crystallographic structure. INTRO | |
| 140 149 β-hairpin structure_element Inspired by these β-hairpin structures, our laboratory developed a macrocyclic β-sheet peptide derived from Aβ17–36 designed to mimic an Aβ β-hairpin and reported its X-ray crystallographic structure. INTRO | |
| 167 199 X-ray crystallographic structure evidence Inspired by these β-hairpin structures, our laboratory developed a macrocyclic β-sheet peptide derived from Aβ17–36 designed to mimic an Aβ β-hairpin and reported its X-ray crystallographic structure. INTRO | |
| 14 23 peptide 1 mutant This peptide (peptide 1) consists of two β-strands comprising Aβ17–23 and Aβ30–36 covalently linked by two δ-linked ornithine (δOrn) β-turn mimics. INTRO | |
| 41 50 β-strands structure_element This peptide (peptide 1) consists of two β-strands comprising Aβ17–23 and Aβ30–36 covalently linked by two δ-linked ornithine (δOrn) β-turn mimics. INTRO | |
| 62 64 Aβ protein This peptide (peptide 1) consists of two β-strands comprising Aβ17–23 and Aβ30–36 covalently linked by two δ-linked ornithine (δOrn) β-turn mimics. INTRO | |
| 64 69 17–23 residue_range This peptide (peptide 1) consists of two β-strands comprising Aβ17–23 and Aβ30–36 covalently linked by two δ-linked ornithine (δOrn) β-turn mimics. INTRO | |
| 74 76 Aβ protein This peptide (peptide 1) consists of two β-strands comprising Aβ17–23 and Aβ30–36 covalently linked by two δ-linked ornithine (δOrn) β-turn mimics. INTRO | |
| 76 81 30–36 residue_range This peptide (peptide 1) consists of two β-strands comprising Aβ17–23 and Aβ30–36 covalently linked by two δ-linked ornithine (δOrn) β-turn mimics. INTRO | |
| 107 115 δ-linked protein_state This peptide (peptide 1) consists of two β-strands comprising Aβ17–23 and Aβ30–36 covalently linked by two δ-linked ornithine (δOrn) β-turn mimics. INTRO | |
| 116 125 ornithine residue_name This peptide (peptide 1) consists of two β-strands comprising Aβ17–23 and Aβ30–36 covalently linked by two δ-linked ornithine (δOrn) β-turn mimics. INTRO | |
| 127 131 δOrn structure_element This peptide (peptide 1) consists of two β-strands comprising Aβ17–23 and Aβ30–36 covalently linked by two δ-linked ornithine (δOrn) β-turn mimics. INTRO | |
| 133 139 β-turn structure_element This peptide (peptide 1) consists of two β-strands comprising Aβ17–23 and Aβ30–36 covalently linked by two δ-linked ornithine (δOrn) β-turn mimics. INTRO | |
| 4 8 δOrn structure_element The δOrn that connects residues D23 and A30 replaces the Aβ24–29 loop. INTRO | |
| 32 35 D23 residue_name_number The δOrn that connects residues D23 and A30 replaces the Aβ24–29 loop. INTRO | |
| 40 43 A30 residue_name_number The δOrn that connects residues D23 and A30 replaces the Aβ24–29 loop. INTRO | |
| 57 59 Aβ protein The δOrn that connects residues D23 and A30 replaces the Aβ24–29 loop. INTRO | |
| 59 64 24–29 residue_range The δOrn that connects residues D23 and A30 replaces the Aβ24–29 loop. INTRO | |
| 65 69 loop structure_element The δOrn that connects residues D23 and A30 replaces the Aβ24–29 loop. INTRO | |
| 4 8 δOrn structure_element The δOrn that connects residues L17 and V36 enforces β-hairpin structure. INTRO | |
| 32 35 L17 residue_name_number The δOrn that connects residues L17 and V36 enforces β-hairpin structure. INTRO | |
| 40 43 V36 residue_name_number The δOrn that connects residues L17 and V36 enforces β-hairpin structure. INTRO | |
| 53 62 β-hairpin structure_element The δOrn that connects residues L17 and V36 enforces β-hairpin structure. INTRO | |
| 46 49 G33 residue_name_number We incorporated an N-methyl group at position G33 to prevent uncontrolled aggregation and precipitation of the peptide. INTRO | |
| 44 52 replaced experimental_method To improve the solubility of the peptide we replaced M35 with the hydrophilic isostere of methionine, ornithine (α-linked) (Figure 1B). INTRO | |
| 53 56 M35 residue_name_number To improve the solubility of the peptide we replaced M35 with the hydrophilic isostere of methionine, ornithine (α-linked) (Figure 1B). INTRO | |
| 90 100 methionine residue_name To improve the solubility of the peptide we replaced M35 with the hydrophilic isostere of methionine, ornithine (α-linked) (Figure 1B). INTRO | |
| 102 111 ornithine residue_name To improve the solubility of the peptide we replaced M35 with the hydrophilic isostere of methionine, ornithine (α-linked) (Figure 1B). INTRO | |
| 113 121 α-linked protein_state To improve the solubility of the peptide we replaced M35 with the hydrophilic isostere of methionine, ornithine (α-linked) (Figure 1B). INTRO | |
| 4 36 X-ray crystallographic structure evidence The X-ray crystallographic structure of peptide 1 reveals that it folds to form a β-hairpin that assembles to form trimers and that the trimers further assemble to form hexamers and dodecamers. INTRO | |
| 40 49 peptide 1 mutant The X-ray crystallographic structure of peptide 1 reveals that it folds to form a β-hairpin that assembles to form trimers and that the trimers further assemble to form hexamers and dodecamers. INTRO | |
| 82 91 β-hairpin structure_element The X-ray crystallographic structure of peptide 1 reveals that it folds to form a β-hairpin that assembles to form trimers and that the trimers further assemble to form hexamers and dodecamers. INTRO | |
| 115 122 trimers oligomeric_state The X-ray crystallographic structure of peptide 1 reveals that it folds to form a β-hairpin that assembles to form trimers and that the trimers further assemble to form hexamers and dodecamers. INTRO | |
| 136 143 trimers oligomeric_state The X-ray crystallographic structure of peptide 1 reveals that it folds to form a β-hairpin that assembles to form trimers and that the trimers further assemble to form hexamers and dodecamers. INTRO | |
| 169 177 hexamers oligomeric_state The X-ray crystallographic structure of peptide 1 reveals that it folds to form a β-hairpin that assembles to form trimers and that the trimers further assemble to form hexamers and dodecamers. INTRO | |
| 182 192 dodecamers oligomeric_state The X-ray crystallographic structure of peptide 1 reveals that it folds to form a β-hairpin that assembles to form trimers and that the trimers further assemble to form hexamers and dodecamers. INTRO | |
| 39 55 peptides 1 and 2 chemical (A) Cartoon illustrating the design of peptides 1 and 2 and their relationship to an Aβ17–36 β-hairpin. FIG | |
| 85 87 Aβ protein (A) Cartoon illustrating the design of peptides 1 and 2 and their relationship to an Aβ17–36 β-hairpin. FIG | |
| 87 92 17–36 residue_range (A) Cartoon illustrating the design of peptides 1 and 2 and their relationship to an Aβ17–36 β-hairpin. FIG | |
| 93 102 β-hairpin structure_element (A) Cartoon illustrating the design of peptides 1 and 2 and their relationship to an Aβ17–36 β-hairpin. FIG | |
| 27 36 peptide 1 mutant (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 50 52 Aβ protein (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 62 64 Aβ protein (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 107 115 δ-linked protein_state (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 116 125 ornithine residue_name (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 126 131 turns structure_element (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 159 168 peptide 2 mutant (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 182 184 Aβ protein (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 215 229 disulfide bond ptm (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 247 249 24 residue_number (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 254 256 29 residue_number (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 266 274 δ-linked protein_state (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 275 284 ornithine residue_name (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 285 289 turn structure_element (B) Chemical structure of peptide 1 illustrating Aβ17–23 and Aβ30–36, M35Orn, the N-methyl group, and the δ-linked ornithine turns. (C) Chemical structure of peptide 2 illustrating Aβ17–36, the N-methyl group, the disulfide bond across positions 24 and 29, and the δ-linked ornithine turn. FIG | |
| 14 23 peptide 1 mutant Our design of peptide 1 omitted the Aβ24–29 loop. INTRO | |
| 36 38 Aβ protein Our design of peptide 1 omitted the Aβ24–29 loop. INTRO | |
| 38 43 24–29 residue_range Our design of peptide 1 omitted the Aβ24–29 loop. INTRO | |
| 44 48 loop structure_element Our design of peptide 1 omitted the Aβ24–29 loop. INTRO | |
| 17 19 Aβ protein To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 19 24 24–29 residue_range To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 25 29 loop structure_element To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 44 79 replica-exchange molecular dynamics experimental_method To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 81 85 REMD experimental_method To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 87 98 simulations experimental_method To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 102 104 Aβ protein To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 104 109 17–36 residue_range To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 120 154 X-ray crystallographic coordinates evidence To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 158 160 Aβ protein To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 160 165 17–23 residue_range To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 170 172 Aβ protein To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 172 177 30–36 residue_range To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 183 192 peptide 1 mutant To visualize the Aβ24–29 loop, we performed replica-exchange molecular dynamics (REMD) simulations on Aβ17–36 using the X-ray crystallographic coordinates of Aβ17–23 and Aβ30–36 from peptide 1. INTRO | |
| 45 51 trimer oligomeric_state These studies provided a working model for a trimer of Aβ17–36 β-hairpins and demonstrated that the trimer should be capable of accommodating the Aβ24–29 loop. INTRO | |
| 55 57 Aβ protein These studies provided a working model for a trimer of Aβ17–36 β-hairpins and demonstrated that the trimer should be capable of accommodating the Aβ24–29 loop. INTRO | |
| 57 62 17–36 residue_range These studies provided a working model for a trimer of Aβ17–36 β-hairpins and demonstrated that the trimer should be capable of accommodating the Aβ24–29 loop. INTRO | |
| 63 73 β-hairpins structure_element These studies provided a working model for a trimer of Aβ17–36 β-hairpins and demonstrated that the trimer should be capable of accommodating the Aβ24–29 loop. INTRO | |
| 100 106 trimer oligomeric_state These studies provided a working model for a trimer of Aβ17–36 β-hairpins and demonstrated that the trimer should be capable of accommodating the Aβ24–29 loop. INTRO | |
| 146 148 Aβ protein These studies provided a working model for a trimer of Aβ17–36 β-hairpins and demonstrated that the trimer should be capable of accommodating the Aβ24–29 loop. INTRO | |
| 148 153 24–29 residue_range These studies provided a working model for a trimer of Aβ17–36 β-hairpins and demonstrated that the trimer should be capable of accommodating the Aβ24–29 loop. INTRO | |
| 154 158 loop structure_element These studies provided a working model for a trimer of Aβ17–36 β-hairpins and demonstrated that the trimer should be capable of accommodating the Aβ24–29 loop. INTRO | |
| 35 42 restore experimental_method In the current study we set out to restore the Aβ24–29 loop, reintroduce the methionine residue at position 35, and determine the X-ray crystallographic structures of oligomers that form. INTRO | |
| 47 49 Aβ protein In the current study we set out to restore the Aβ24–29 loop, reintroduce the methionine residue at position 35, and determine the X-ray crystallographic structures of oligomers that form. INTRO | |
| 49 54 24–29 residue_range In the current study we set out to restore the Aβ24–29 loop, reintroduce the methionine residue at position 35, and determine the X-ray crystallographic structures of oligomers that form. INTRO | |
| 55 59 loop structure_element In the current study we set out to restore the Aβ24–29 loop, reintroduce the methionine residue at position 35, and determine the X-ray crystallographic structures of oligomers that form. INTRO | |
| 61 72 reintroduce experimental_method In the current study we set out to restore the Aβ24–29 loop, reintroduce the methionine residue at position 35, and determine the X-ray crystallographic structures of oligomers that form. INTRO | |
| 77 87 methionine residue_name In the current study we set out to restore the Aβ24–29 loop, reintroduce the methionine residue at position 35, and determine the X-ray crystallographic structures of oligomers that form. INTRO | |
| 108 110 35 residue_number In the current study we set out to restore the Aβ24–29 loop, reintroduce the methionine residue at position 35, and determine the X-ray crystallographic structures of oligomers that form. INTRO | |
| 130 163 X-ray crystallographic structures evidence In the current study we set out to restore the Aβ24–29 loop, reintroduce the methionine residue at position 35, and determine the X-ray crystallographic structures of oligomers that form. INTRO | |
| 167 176 oligomers oligomeric_state In the current study we set out to restore the Aβ24–29 loop, reintroduce the methionine residue at position 35, and determine the X-ray crystallographic structures of oligomers that form. INTRO | |
| 12 21 peptide 2 mutant We designed peptide 2 as a homologue of peptide 1 that embodies these ideas. INTRO | |
| 40 49 peptide 1 mutant We designed peptide 2 as a homologue of peptide 1 that embodies these ideas. INTRO | |
| 0 9 Peptide 2 mutant Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 21 31 methionine residue_name Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 52 54 35 residue_number Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 62 64 Aβ protein Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 64 69 24–29 residue_range Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 70 74 loop structure_element Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 89 91 24 residue_number Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 96 98 29 residue_number Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 100 103 Val residue_name Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 108 111 Gly residue_name Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 113 120 mutated experimental_method Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 124 132 cysteine residue_name Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 149 163 disulfide bond ptm Peptide 2 contains a methionine residue at position 35 and an Aβ24–29 loop with residues 24 and 29 (Val and Gly) mutated to cysteine and linked by a disulfide bond (Figure 1C). INTRO | |
| 37 46 peptide 2 mutant Here, we describe the development of peptide 2 and report the X-ray crystallographic structures of the trimer, dodecamer, and annular pore observed within the crystal structure. INTRO | |
| 62 95 X-ray crystallographic structures evidence Here, we describe the development of peptide 2 and report the X-ray crystallographic structures of the trimer, dodecamer, and annular pore observed within the crystal structure. INTRO | |
| 103 109 trimer oligomeric_state Here, we describe the development of peptide 2 and report the X-ray crystallographic structures of the trimer, dodecamer, and annular pore observed within the crystal structure. INTRO | |
| 111 120 dodecamer oligomeric_state Here, we describe the development of peptide 2 and report the X-ray crystallographic structures of the trimer, dodecamer, and annular pore observed within the crystal structure. INTRO | |
| 126 138 annular pore site Here, we describe the development of peptide 2 and report the X-ray crystallographic structures of the trimer, dodecamer, and annular pore observed within the crystal structure. INTRO | |
| 159 176 crystal structure evidence Here, we describe the development of peptide 2 and report the X-ray crystallographic structures of the trimer, dodecamer, and annular pore observed within the crystal structure. INTRO | |
| 15 24 Peptide 2 mutant Development of Peptide 2 RESULTS | |
| 13 22 peptide 2 mutant We developed peptide 2 from peptide 1 by an iterative process, in which we first attempted to restore the Aβ24–29 loop without a disulfide linkage. RESULTS | |
| 28 37 peptide 1 mutant We developed peptide 2 from peptide 1 by an iterative process, in which we first attempted to restore the Aβ24–29 loop without a disulfide linkage. RESULTS | |
| 106 108 Aβ protein We developed peptide 2 from peptide 1 by an iterative process, in which we first attempted to restore the Aβ24–29 loop without a disulfide linkage. RESULTS | |
| 108 113 24–29 residue_range We developed peptide 2 from peptide 1 by an iterative process, in which we first attempted to restore the Aβ24–29 loop without a disulfide linkage. RESULTS | |
| 114 118 loop structure_element We developed peptide 2 from peptide 1 by an iterative process, in which we first attempted to restore the Aβ24–29 loop without a disulfide linkage. RESULTS | |
| 129 146 disulfide linkage ptm We developed peptide 2 from peptide 1 by an iterative process, in which we first attempted to restore the Aβ24–29 loop without a disulfide linkage. RESULTS | |
| 14 23 peptide 3 mutant We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 42 51 peptide 1 mutant We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 61 63 Aβ protein We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 63 68 24–29 residue_range We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 69 73 loop structure_element We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 90 94 δOrn structure_element We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 109 112 D23 residue_name_number We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 117 120 A30 residue_name_number We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 125 144 p-iodophenylalanine chemical We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 146 148 FI chemical We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 162 165 F19 residue_name_number We envisioned peptide 3 as a homologue of peptide 1 with the Aβ24–29 loop in place of the δOrn that connects D23 and A30 and p-iodophenylalanine (FI) in place of F19. RESULTS | |
| 17 36 p-iodophenylalanine chemical We routinely use p-iodophenylalanine to determine the X-ray crystallographic phases. RESULTS | |
| 54 83 X-ray crystallographic phases evidence We routinely use p-iodophenylalanine to determine the X-ray crystallographic phases. RESULTS | |
| 22 54 X-ray crystallographic structure evidence After determining the X-ray crystallographic structure of the p-iodophenylalanine variant we attempt to determine the structure of the native phenylalanine compound by isomorphous replacement. RESULTS | |
| 62 81 p-iodophenylalanine chemical After determining the X-ray crystallographic structure of the p-iodophenylalanine variant we attempt to determine the structure of the native phenylalanine compound by isomorphous replacement. RESULTS | |
| 118 127 structure evidence After determining the X-ray crystallographic structure of the p-iodophenylalanine variant we attempt to determine the structure of the native phenylalanine compound by isomorphous replacement. RESULTS | |
| 142 155 phenylalanine residue_name After determining the X-ray crystallographic structure of the p-iodophenylalanine variant we attempt to determine the structure of the native phenylalanine compound by isomorphous replacement. RESULTS | |
| 168 191 isomorphous replacement experimental_method After determining the X-ray crystallographic structure of the p-iodophenylalanine variant we attempt to determine the structure of the native phenylalanine compound by isomorphous replacement. RESULTS | |
| 18 27 peptide 3 mutant Upon synthesizing peptide 3, we found that it formed an amorphous precipitate in most crystallization conditions screened and failed to afford crystals in any condition. RESULTS | |
| 143 151 crystals evidence Upon synthesizing peptide 3, we found that it formed an amorphous precipitate in most crystallization conditions screened and failed to afford crystals in any condition. RESULTS | |
| 34 38 δOrn structure_element We postulate that the loss of the δOrn constraint leads to conformational heterogeneity that prevents peptide 3 from crystallizing. RESULTS | |
| 102 111 peptide 3 mutant We postulate that the loss of the δOrn constraint leads to conformational heterogeneity that prevents peptide 3 from crystallizing. RESULTS | |
| 46 60 disulfide bond ptm To address this issue, we next incorporated a disulfide bond between residues 24 and 29 as a conformational constraint that serves as a surrogate for δOrn. RESULTS | |
| 78 80 24 residue_number To address this issue, we next incorporated a disulfide bond between residues 24 and 29 as a conformational constraint that serves as a surrogate for δOrn. RESULTS | |
| 85 87 29 residue_number To address this issue, we next incorporated a disulfide bond between residues 24 and 29 as a conformational constraint that serves as a surrogate for δOrn. RESULTS | |
| 150 154 δOrn structure_element To address this issue, we next incorporated a disulfide bond between residues 24 and 29 as a conformational constraint that serves as a surrogate for δOrn. RESULTS | |
| 12 21 peptide 4 mutant We designed peptide 4 to embody this idea, mutating Val24 and Gly29 to cysteine and forming an interstrand disulfide linkage. RESULTS | |
| 43 51 mutating experimental_method We designed peptide 4 to embody this idea, mutating Val24 and Gly29 to cysteine and forming an interstrand disulfide linkage. RESULTS | |
| 52 57 Val24 residue_name_number We designed peptide 4 to embody this idea, mutating Val24 and Gly29 to cysteine and forming an interstrand disulfide linkage. RESULTS | |
| 62 67 Gly29 residue_name_number We designed peptide 4 to embody this idea, mutating Val24 and Gly29 to cysteine and forming an interstrand disulfide linkage. RESULTS | |
| 71 79 cysteine residue_name We designed peptide 4 to embody this idea, mutating Val24 and Gly29 to cysteine and forming an interstrand disulfide linkage. RESULTS | |
| 107 124 disulfide linkage ptm We designed peptide 4 to embody this idea, mutating Val24 and Gly29 to cysteine and forming an interstrand disulfide linkage. RESULTS | |
| 3 10 mutated experimental_method We mutated these residues because they occupy the same position as the δOrn that connects D23 and A30 in peptide 1. RESULTS | |
| 71 75 δOrn structure_element We mutated these residues because they occupy the same position as the δOrn that connects D23 and A30 in peptide 1. RESULTS | |
| 90 93 D23 residue_name_number We mutated these residues because they occupy the same position as the δOrn that connects D23 and A30 in peptide 1. RESULTS | |
| 98 101 A30 residue_name_number We mutated these residues because they occupy the same position as the δOrn that connects D23 and A30 in peptide 1. RESULTS | |
| 105 114 peptide 1 mutant We mutated these residues because they occupy the same position as the δOrn that connects D23 and A30 in peptide 1. RESULTS | |
| 9 12 V24 residue_name_number Residues V24 and G29 form a non-hydrogen-bonded pair, which can readily accommodate disulfide linkages in antiparallel β-sheets. RESULTS | |
| 17 20 G29 residue_name_number Residues V24 and G29 form a non-hydrogen-bonded pair, which can readily accommodate disulfide linkages in antiparallel β-sheets. RESULTS | |
| 28 52 non-hydrogen-bonded pair bond_interaction Residues V24 and G29 form a non-hydrogen-bonded pair, which can readily accommodate disulfide linkages in antiparallel β-sheets. RESULTS | |
| 84 102 disulfide linkages ptm Residues V24 and G29 form a non-hydrogen-bonded pair, which can readily accommodate disulfide linkages in antiparallel β-sheets. RESULTS | |
| 106 127 antiparallel β-sheets structure_element Residues V24 and G29 form a non-hydrogen-bonded pair, which can readily accommodate disulfide linkages in antiparallel β-sheets. RESULTS | |
| 0 15 Disulfide bonds ptm Disulfide bonds across non-hydrogen-bonded pairs stabilize β-hairpins, while disulfide bonds across hydrogen-bonded pairs do not. RESULTS | |
| 23 48 non-hydrogen-bonded pairs bond_interaction Disulfide bonds across non-hydrogen-bonded pairs stabilize β-hairpins, while disulfide bonds across hydrogen-bonded pairs do not. RESULTS | |
| 59 69 β-hairpins structure_element Disulfide bonds across non-hydrogen-bonded pairs stabilize β-hairpins, while disulfide bonds across hydrogen-bonded pairs do not. RESULTS | |
| 77 92 disulfide bonds ptm Disulfide bonds across non-hydrogen-bonded pairs stabilize β-hairpins, while disulfide bonds across hydrogen-bonded pairs do not. RESULTS | |
| 100 121 hydrogen-bonded pairs bond_interaction Disulfide bonds across non-hydrogen-bonded pairs stabilize β-hairpins, while disulfide bonds across hydrogen-bonded pairs do not. RESULTS | |
| 13 27 disulfide bond ptm Although the disulfide bond between positions 24 and 29 helps stabilize the β-hairpin, it does not alter the charge or substantially change the hydrophobicity of the Aβ17–36 β-hairpin. RESULTS | |
| 46 48 24 residue_number Although the disulfide bond between positions 24 and 29 helps stabilize the β-hairpin, it does not alter the charge or substantially change the hydrophobicity of the Aβ17–36 β-hairpin. RESULTS | |
| 53 55 29 residue_number Although the disulfide bond between positions 24 and 29 helps stabilize the β-hairpin, it does not alter the charge or substantially change the hydrophobicity of the Aβ17–36 β-hairpin. RESULTS | |
| 76 85 β-hairpin structure_element Although the disulfide bond between positions 24 and 29 helps stabilize the β-hairpin, it does not alter the charge or substantially change the hydrophobicity of the Aβ17–36 β-hairpin. RESULTS | |
| 166 168 Aβ protein Although the disulfide bond between positions 24 and 29 helps stabilize the β-hairpin, it does not alter the charge or substantially change the hydrophobicity of the Aβ17–36 β-hairpin. RESULTS | |
| 168 173 17–36 residue_range Although the disulfide bond between positions 24 and 29 helps stabilize the β-hairpin, it does not alter the charge or substantially change the hydrophobicity of the Aβ17–36 β-hairpin. RESULTS | |
| 174 183 β-hairpin structure_element Although the disulfide bond between positions 24 and 29 helps stabilize the β-hairpin, it does not alter the charge or substantially change the hydrophobicity of the Aβ17–36 β-hairpin. RESULTS | |
| 31 40 peptide 4 mutant We were gratified to find that peptide 4 afforded crystals suitable for X-ray crystallography. RESULTS | |
| 50 58 crystals evidence We were gratified to find that peptide 4 afforded crystals suitable for X-ray crystallography. RESULTS | |
| 72 93 X-ray crystallography experimental_method We were gratified to find that peptide 4 afforded crystals suitable for X-ray crystallography. RESULTS | |
| 46 56 determined experimental_method As the next step in the iterative process, we determined the X-ray crystallographic structure of this peptide (PDB 5HOW). RESULTS | |
| 61 93 X-ray crystallographic structure evidence As the next step in the iterative process, we determined the X-ray crystallographic structure of this peptide (PDB 5HOW). RESULTS | |
| 22 54 X-ray crystallographic structure evidence After determining the X-ray crystallographic structure of peptide 4 we reintroduced the native phenylalanine at position 19 and the methionine at position 35 to afford peptide 2. RESULTS | |
| 58 67 peptide 4 mutant After determining the X-ray crystallographic structure of peptide 4 we reintroduced the native phenylalanine at position 19 and the methionine at position 35 to afford peptide 2. RESULTS | |
| 71 83 reintroduced experimental_method After determining the X-ray crystallographic structure of peptide 4 we reintroduced the native phenylalanine at position 19 and the methionine at position 35 to afford peptide 2. RESULTS | |
| 95 108 phenylalanine residue_name After determining the X-ray crystallographic structure of peptide 4 we reintroduced the native phenylalanine at position 19 and the methionine at position 35 to afford peptide 2. RESULTS | |
| 121 123 19 residue_number After determining the X-ray crystallographic structure of peptide 4 we reintroduced the native phenylalanine at position 19 and the methionine at position 35 to afford peptide 2. RESULTS | |
| 132 142 methionine residue_name After determining the X-ray crystallographic structure of peptide 4 we reintroduced the native phenylalanine at position 19 and the methionine at position 35 to afford peptide 2. RESULTS | |
| 155 157 35 residue_number After determining the X-ray crystallographic structure of peptide 4 we reintroduced the native phenylalanine at position 19 and the methionine at position 35 to afford peptide 2. RESULTS | |
| 168 177 peptide 2 mutant After determining the X-ray crystallographic structure of peptide 4 we reintroduced the native phenylalanine at position 19 and the methionine at position 35 to afford peptide 2. RESULTS | |
| 89 121 X-ray crystallographic structure evidence We completed the iterative process—from 1 to 3 to 4 to 2—by successfully determining the X-ray crystallographic structure of peptide 2 (PDB 5HOX and 5HOY). RESULTS | |
| 125 134 peptide 2 mutant We completed the iterative process—from 1 to 3 to 4 to 2—by successfully determining the X-ray crystallographic structure of peptide 2 (PDB 5HOX and 5HOY). RESULTS | |
| 49 61 peptides 2–4 mutant The following sections describe the synthesis of peptides 2–4 and the X-ray crystallographic structure of peptide 2. RESULTS | |
| 70 102 X-ray crystallographic structure evidence The following sections describe the synthesis of peptides 2–4 and the X-ray crystallographic structure of peptide 2. RESULTS | |
| 106 115 peptide 2 mutant The following sections describe the synthesis of peptides 2–4 and the X-ray crystallographic structure of peptide 2. RESULTS | |
| 13 25 Peptides 2–4 mutant Synthesis of Peptides 2–4 RESULTS | |
| 15 27 peptides 2–4 mutant We synthesized peptides 2–4 by similar procedures to those we have developed for other macrocyclic peptides. RESULTS | |
| 16 32 peptides 2 and 4 mutant In synthesizing peptides 2 and 4 we formed the disulfide linkage after macrolactamization and deprotection of the acid-labile side chain protecting groups. RESULTS | |
| 47 64 disulfide linkage ptm In synthesizing peptides 2 and 4 we formed the disulfide linkage after macrolactamization and deprotection of the acid-labile side chain protecting groups. RESULTS | |
| 8 19 acid-stable protein_state We used acid-stable Acm-protected cysteine residues at positions 24 and 29 and removed the Acm groups by oxidation with I2 in aqueous acetic acid to afford the disulfide linkage. RESULTS | |
| 20 33 Acm-protected protein_state We used acid-stable Acm-protected cysteine residues at positions 24 and 29 and removed the Acm groups by oxidation with I2 in aqueous acetic acid to afford the disulfide linkage. RESULTS | |
| 34 42 cysteine residue_name We used acid-stable Acm-protected cysteine residues at positions 24 and 29 and removed the Acm groups by oxidation with I2 in aqueous acetic acid to afford the disulfide linkage. RESULTS | |
| 65 67 24 residue_number We used acid-stable Acm-protected cysteine residues at positions 24 and 29 and removed the Acm groups by oxidation with I2 in aqueous acetic acid to afford the disulfide linkage. RESULTS | |
| 72 74 29 residue_number We used acid-stable Acm-protected cysteine residues at positions 24 and 29 and removed the Acm groups by oxidation with I2 in aqueous acetic acid to afford the disulfide linkage. RESULTS | |
| 134 145 acetic acid chemical We used acid-stable Acm-protected cysteine residues at positions 24 and 29 and removed the Acm groups by oxidation with I2 in aqueous acetic acid to afford the disulfide linkage. RESULTS | |
| 160 177 disulfide linkage ptm We used acid-stable Acm-protected cysteine residues at positions 24 and 29 and removed the Acm groups by oxidation with I2 in aqueous acetic acid to afford the disulfide linkage. RESULTS | |
| 0 12 Peptides 2–4 mutant Peptides 2–4 were purified by RP-HPLC. RESULTS | |
| 30 37 RP-HPLC experimental_method Peptides 2–4 were purified by RP-HPLC. RESULTS | |
| 0 15 Crystallization experimental_method Crystallization, X-ray Crystallographic Data Collection, Data Processing, and Structure Determination of Peptides 2 and 4 RESULTS | |
| 17 55 X-ray Crystallographic Data Collection experimental_method Crystallization, X-ray Crystallographic Data Collection, Data Processing, and Structure Determination of Peptides 2 and 4 RESULTS | |
| 78 101 Structure Determination experimental_method Crystallization, X-ray Crystallographic Data Collection, Data Processing, and Structure Determination of Peptides 2 and 4 RESULTS | |
| 105 121 Peptides 2 and 4 mutant Crystallization, X-ray Crystallographic Data Collection, Data Processing, and Structure Determination of Peptides 2 and 4 RESULTS | |
| 3 38 screened crystallization conditions experimental_method We screened crystallization conditions for peptide 4 in a 96-well-plate format using three different Hampton Research crystallization kits (Crystal Screen, Index, and PEG/Ion) with three ratios of peptide and mother liquor per condition (864 experiments). RESULTS | |
| 43 52 peptide 4 mutant We screened crystallization conditions for peptide 4 in a 96-well-plate format using three different Hampton Research crystallization kits (Crystal Screen, Index, and PEG/Ion) with three ratios of peptide and mother liquor per condition (864 experiments). RESULTS | |
| 0 9 Peptide 4 mutant Peptide 4 afforded crystals in a single set of conditions containing HEPES buffer and Jeffamine M-600—the same crystallization conditions that afforded crystals of peptide 1. RESULTS | |
| 19 27 crystals evidence Peptide 4 afforded crystals in a single set of conditions containing HEPES buffer and Jeffamine M-600—the same crystallization conditions that afforded crystals of peptide 1. RESULTS | |
| 86 101 Jeffamine M-600 chemical Peptide 4 afforded crystals in a single set of conditions containing HEPES buffer and Jeffamine M-600—the same crystallization conditions that afforded crystals of peptide 1. RESULTS | |
| 152 160 crystals evidence Peptide 4 afforded crystals in a single set of conditions containing HEPES buffer and Jeffamine M-600—the same crystallization conditions that afforded crystals of peptide 1. RESULTS | |
| 164 173 peptide 1 mutant Peptide 4 afforded crystals in a single set of conditions containing HEPES buffer and Jeffamine M-600—the same crystallization conditions that afforded crystals of peptide 1. RESULTS | |
| 0 9 Peptide 2 mutant Peptide 2 also afforded crystals in these conditions. RESULTS | |
| 24 32 crystals evidence Peptide 2 also afforded crystals in these conditions. RESULTS | |
| 63 71 crystals evidence We further optimized these conditions to rapidly (∼72 h) yield crystals suitable for X-ray crystallography. RESULTS | |
| 85 106 X-ray crystallography experimental_method We further optimized these conditions to rapidly (∼72 h) yield crystals suitable for X-ray crystallography. RESULTS | |
| 42 47 HEPES chemical The optimized conditions consist of 0.1 M HEPES at pH 6.4 with 31% Jeffamine M-600 for peptide 4 and 0.1 M HEPES pH 7.1 with 29% Jeffamine M-600 for peptide 2. RESULTS | |
| 67 82 Jeffamine M-600 chemical The optimized conditions consist of 0.1 M HEPES at pH 6.4 with 31% Jeffamine M-600 for peptide 4 and 0.1 M HEPES pH 7.1 with 29% Jeffamine M-600 for peptide 2. RESULTS | |
| 87 96 peptide 4 mutant The optimized conditions consist of 0.1 M HEPES at pH 6.4 with 31% Jeffamine M-600 for peptide 4 and 0.1 M HEPES pH 7.1 with 29% Jeffamine M-600 for peptide 2. RESULTS | |
| 107 112 HEPES chemical The optimized conditions consist of 0.1 M HEPES at pH 6.4 with 31% Jeffamine M-600 for peptide 4 and 0.1 M HEPES pH 7.1 with 29% Jeffamine M-600 for peptide 2. RESULTS | |
| 129 144 Jeffamine M-600 chemical The optimized conditions consist of 0.1 M HEPES at pH 6.4 with 31% Jeffamine M-600 for peptide 4 and 0.1 M HEPES pH 7.1 with 29% Jeffamine M-600 for peptide 2. RESULTS | |
| 149 158 peptide 2 mutant The optimized conditions consist of 0.1 M HEPES at pH 6.4 with 31% Jeffamine M-600 for peptide 4 and 0.1 M HEPES pH 7.1 with 29% Jeffamine M-600 for peptide 2. RESULTS | |
| 0 24 Crystal diffraction data evidence Crystal diffraction data for peptides 4 and 2 were collected in-house with a Rigaku MicroMax 007HF X-ray diffractometer at 1.54 Å wavelength. RESULTS | |
| 29 45 peptides 4 and 2 mutant Crystal diffraction data for peptides 4 and 2 were collected in-house with a Rigaku MicroMax 007HF X-ray diffractometer at 1.54 Å wavelength. RESULTS | |
| 0 24 Crystal diffraction data evidence Crystal diffraction data for peptide 2 were also collected at the Advanced Light Source at Lawrence Berkeley National Laboratory with a synchrotron source at 1.00 Å wavelength to achieve higher resolution. RESULTS | |
| 29 38 peptide 2 mutant Crystal diffraction data for peptide 2 were also collected at the Advanced Light Source at Lawrence Berkeley National Laboratory with a synchrotron source at 1.00 Å wavelength to achieve higher resolution. RESULTS | |
| 10 26 peptides 4 and 2 mutant Data from peptides 4 and 2 suitable for refinement at 2.30 Å were obtained from the diffractometer; data from peptide 2 suitable for refinement at 1.90 Å were obtained from the synchrotron. RESULTS | |
| 110 119 peptide 2 mutant Data from peptides 4 and 2 suitable for refinement at 2.30 Å were obtained from the diffractometer; data from peptide 2 suitable for refinement at 1.90 Å were obtained from the synchrotron. RESULTS | |
| 9 25 peptides 4 and 2 mutant Data for peptides 4 and 2 were scaled and merged using XDS. RESULTS | |
| 0 6 Phases evidence Phases for peptide 4 were determined by single-wavelength anomalous diffraction (SAD) phasing by using the coordinates of the iodine anomalous signal from p-iodophenylalanine. RESULTS | |
| 11 20 peptide 4 mutant Phases for peptide 4 were determined by single-wavelength anomalous diffraction (SAD) phasing by using the coordinates of the iodine anomalous signal from p-iodophenylalanine. RESULTS | |
| 40 79 single-wavelength anomalous diffraction experimental_method Phases for peptide 4 were determined by single-wavelength anomalous diffraction (SAD) phasing by using the coordinates of the iodine anomalous signal from p-iodophenylalanine. RESULTS | |
| 81 84 SAD experimental_method Phases for peptide 4 were determined by single-wavelength anomalous diffraction (SAD) phasing by using the coordinates of the iodine anomalous signal from p-iodophenylalanine. RESULTS | |
| 86 93 phasing experimental_method Phases for peptide 4 were determined by single-wavelength anomalous diffraction (SAD) phasing by using the coordinates of the iodine anomalous signal from p-iodophenylalanine. RESULTS | |
| 126 149 iodine anomalous signal evidence Phases for peptide 4 were determined by single-wavelength anomalous diffraction (SAD) phasing by using the coordinates of the iodine anomalous signal from p-iodophenylalanine. RESULTS | |
| 155 174 p-iodophenylalanine chemical Phases for peptide 4 were determined by single-wavelength anomalous diffraction (SAD) phasing by using the coordinates of the iodine anomalous signal from p-iodophenylalanine. RESULTS | |
| 0 6 Phases evidence Phases for peptide 2 were determined by isomorphous replacement of peptide 4. RESULTS | |
| 11 20 peptide 2 mutant Phases for peptide 2 were determined by isomorphous replacement of peptide 4. RESULTS | |
| 40 63 isomorphous replacement experimental_method Phases for peptide 2 were determined by isomorphous replacement of peptide 4. RESULTS | |
| 67 76 peptide 4 mutant Phases for peptide 2 were determined by isomorphous replacement of peptide 4. RESULTS | |
| 4 14 structures evidence The structures of peptides 2 and 4 were solved and refined in the P6122 space group. RESULTS | |
| 18 34 peptides 2 and 4 mutant The structures of peptides 2 and 4 were solved and refined in the P6122 space group. RESULTS | |
| 40 46 solved experimental_method The structures of peptides 2 and 4 were solved and refined in the P6122 space group. RESULTS | |
| 28 35 peptide chemical The asymmetric unit of each peptide consists of six monomers, arranged as two trimers. RESULTS | |
| 52 60 monomers oligomeric_state The asymmetric unit of each peptide consists of six monomers, arranged as two trimers. RESULTS | |
| 78 85 trimers oligomeric_state The asymmetric unit of each peptide consists of six monomers, arranged as two trimers. RESULTS | |
| 0 16 Peptides 2 and 4 mutant Peptides 2 and 4 form morphologically identical structures and assemblies in the crystal lattice. RESULTS | |
| 81 96 crystal lattice evidence Peptides 2 and 4 form morphologically identical structures and assemblies in the crystal lattice. RESULTS | |
| 0 32 X-ray Crystallographic Structure evidence X-ray Crystallographic Structure of Peptide 2 and the Oligomers It Forms RESULTS | |
| 36 45 Peptide 2 mutant X-ray Crystallographic Structure of Peptide 2 and the Oligomers It Forms RESULTS | |
| 54 63 Oligomers oligomeric_state X-ray Crystallographic Structure of Peptide 2 and the Oligomers It Forms RESULTS | |
| 4 36 X-ray crystallographic structure evidence The X-ray crystallographic structure of peptide 2 reveals that it folds to form a twisted β-hairpin comprising two β-strands connected by a loop (Figure 2A). RESULTS | |
| 40 49 peptide 2 mutant The X-ray crystallographic structure of peptide 2 reveals that it folds to form a twisted β-hairpin comprising two β-strands connected by a loop (Figure 2A). RESULTS | |
| 82 99 twisted β-hairpin structure_element The X-ray crystallographic structure of peptide 2 reveals that it folds to form a twisted β-hairpin comprising two β-strands connected by a loop (Figure 2A). RESULTS | |
| 115 124 β-strands structure_element The X-ray crystallographic structure of peptide 2 reveals that it folds to form a twisted β-hairpin comprising two β-strands connected by a loop (Figure 2A). RESULTS | |
| 140 144 loop structure_element The X-ray crystallographic structure of peptide 2 reveals that it folds to form a twisted β-hairpin comprising two β-strands connected by a loop (Figure 2A). RESULTS | |
| 43 52 β-hairpin structure_element Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 54 57 L17 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 59 62 F19 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 64 67 A21 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 69 72 D23 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 74 77 A30 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 79 82 I32 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 84 87 L34 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 93 96 V36 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 118 121 V18 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 123 126 F20 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 128 131 E22 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 133 136 C24 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 138 141 C29 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 143 146 I31 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 148 151 G33 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 157 160 M35 residue_name_number Eight residues make up each surface of the β-hairpin: L17, F19, A21, D23, A30, I32, L34, and V36 make up one surface; V18, F20, E22, C24, C29, I31, G33, and M35 make up the other surface. RESULTS | |
| 4 13 β-strands structure_element The β-strands of the monomers in the asymmetric unit are virtually identical, differing primarily in rotamers of F20, E22, C24, C29, I31, and M35 (Figure S1). RESULTS | |
| 21 29 monomers oligomeric_state The β-strands of the monomers in the asymmetric unit are virtually identical, differing primarily in rotamers of F20, E22, C24, C29, I31, and M35 (Figure S1). RESULTS | |
| 113 116 F20 residue_name_number The β-strands of the monomers in the asymmetric unit are virtually identical, differing primarily in rotamers of F20, E22, C24, C29, I31, and M35 (Figure S1). RESULTS | |
| 118 121 E22 residue_name_number The β-strands of the monomers in the asymmetric unit are virtually identical, differing primarily in rotamers of F20, E22, C24, C29, I31, and M35 (Figure S1). RESULTS | |
| 123 126 C24 residue_name_number The β-strands of the monomers in the asymmetric unit are virtually identical, differing primarily in rotamers of F20, E22, C24, C29, I31, and M35 (Figure S1). RESULTS | |
| 128 131 C29 residue_name_number The β-strands of the monomers in the asymmetric unit are virtually identical, differing primarily in rotamers of F20, E22, C24, C29, I31, and M35 (Figure S1). RESULTS | |
| 133 136 I31 residue_name_number The β-strands of the monomers in the asymmetric unit are virtually identical, differing primarily in rotamers of F20, E22, C24, C29, I31, and M35 (Figure S1). RESULTS | |
| 142 145 M35 residue_name_number The β-strands of the monomers in the asymmetric unit are virtually identical, differing primarily in rotamers of F20, E22, C24, C29, I31, and M35 (Figure S1). RESULTS | |
| 4 22 disulfide linkages ptm The disulfide linkages suffered radiation damage under synchrotron radiation. RESULTS | |
| 3 10 refined experimental_method We refined three of the β-hairpins with intact disulfide linkages and three with thiols to represent cleaved disulfide linkages in the synchrotron data set (PDB 5HOX). RESULTS | |
| 24 34 β-hairpins structure_element We refined three of the β-hairpins with intact disulfide linkages and three with thiols to represent cleaved disulfide linkages in the synchrotron data set (PDB 5HOX). RESULTS | |
| 40 46 intact protein_state We refined three of the β-hairpins with intact disulfide linkages and three with thiols to represent cleaved disulfide linkages in the synchrotron data set (PDB 5HOX). RESULTS | |
| 47 65 disulfide linkages ptm We refined three of the β-hairpins with intact disulfide linkages and three with thiols to represent cleaved disulfide linkages in the synchrotron data set (PDB 5HOX). RESULTS | |
| 101 108 cleaved protein_state We refined three of the β-hairpins with intact disulfide linkages and three with thiols to represent cleaved disulfide linkages in the synchrotron data set (PDB 5HOX). RESULTS | |
| 109 127 disulfide linkages ptm We refined three of the β-hairpins with intact disulfide linkages and three with thiols to represent cleaved disulfide linkages in the synchrotron data set (PDB 5HOX). RESULTS | |
| 32 42 disulfides ptm No evidence for cleavage of the disulfides was observed in the refinement of the data set collected on the X-ray diffractometer, and we refined all disulfide linkages as intact (PDB 5HOY). RESULTS | |
| 63 73 refinement experimental_method No evidence for cleavage of the disulfides was observed in the refinement of the data set collected on the X-ray diffractometer, and we refined all disulfide linkages as intact (PDB 5HOY). RESULTS | |
| 136 143 refined experimental_method No evidence for cleavage of the disulfides was observed in the refinement of the data set collected on the X-ray diffractometer, and we refined all disulfide linkages as intact (PDB 5HOY). RESULTS | |
| 148 166 disulfide linkages ptm No evidence for cleavage of the disulfides was observed in the refinement of the data set collected on the X-ray diffractometer, and we refined all disulfide linkages as intact (PDB 5HOY). RESULTS | |
| 170 176 intact protein_state No evidence for cleavage of the disulfides was observed in the refinement of the data set collected on the X-ray diffractometer, and we refined all disulfide linkages as intact (PDB 5HOY). RESULTS | |
| 36 45 peptide 2 mutant X-ray crystallographic structure of peptide 2 (PDB 5HOX, synchrotron data set). (A) X-ray crystallographic structure of a representative β-hairpin monomer formed by peptide 2. (B) Overlay of the six β-hairpin monomers in the asymmetric unit. FIG | |
| 84 116 X-ray crystallographic structure evidence X-ray crystallographic structure of peptide 2 (PDB 5HOX, synchrotron data set). (A) X-ray crystallographic structure of a representative β-hairpin monomer formed by peptide 2. (B) Overlay of the six β-hairpin monomers in the asymmetric unit. FIG | |
| 137 146 β-hairpin structure_element X-ray crystallographic structure of peptide 2 (PDB 5HOX, synchrotron data set). (A) X-ray crystallographic structure of a representative β-hairpin monomer formed by peptide 2. (B) Overlay of the six β-hairpin monomers in the asymmetric unit. FIG | |
| 147 154 monomer oligomeric_state X-ray crystallographic structure of peptide 2 (PDB 5HOX, synchrotron data set). (A) X-ray crystallographic structure of a representative β-hairpin monomer formed by peptide 2. (B) Overlay of the six β-hairpin monomers in the asymmetric unit. FIG | |
| 165 174 peptide 2 mutant X-ray crystallographic structure of peptide 2 (PDB 5HOX, synchrotron data set). (A) X-ray crystallographic structure of a representative β-hairpin monomer formed by peptide 2. (B) Overlay of the six β-hairpin monomers in the asymmetric unit. FIG | |
| 180 187 Overlay experimental_method X-ray crystallographic structure of peptide 2 (PDB 5HOX, synchrotron data set). (A) X-ray crystallographic structure of a representative β-hairpin monomer formed by peptide 2. (B) Overlay of the six β-hairpin monomers in the asymmetric unit. FIG | |
| 199 208 β-hairpin structure_element X-ray crystallographic structure of peptide 2 (PDB 5HOX, synchrotron data set). (A) X-ray crystallographic structure of a representative β-hairpin monomer formed by peptide 2. (B) Overlay of the six β-hairpin monomers in the asymmetric unit. FIG | |
| 209 217 monomers oligomeric_state X-ray crystallographic structure of peptide 2 (PDB 5HOX, synchrotron data set). (A) X-ray crystallographic structure of a representative β-hairpin monomer formed by peptide 2. (B) Overlay of the six β-hairpin monomers in the asymmetric unit. FIG | |
| 4 14 β-hairpins structure_element The β-hairpins are shown as cartoons to illustrate the differences in the Aβ25–28 loops. FIG | |
| 74 76 Aβ protein The β-hairpins are shown as cartoons to illustrate the differences in the Aβ25–28 loops. FIG | |
| 76 81 25–28 residue_range The β-hairpins are shown as cartoons to illustrate the differences in the Aβ25–28 loops. FIG | |
| 82 87 loops structure_element The β-hairpins are shown as cartoons to illustrate the differences in the Aβ25–28 loops. FIG | |
| 4 6 Aβ protein The Aβ25–28 loops of the six monomers within the asymmetric unit vary substantially in backbone geometry and side chain rotamers (Figures 2B and S1). RESULTS | |
| 6 11 25–28 residue_range The Aβ25–28 loops of the six monomers within the asymmetric unit vary substantially in backbone geometry and side chain rotamers (Figures 2B and S1). RESULTS | |
| 12 17 loops structure_element The Aβ25–28 loops of the six monomers within the asymmetric unit vary substantially in backbone geometry and side chain rotamers (Figures 2B and S1). RESULTS | |
| 29 37 monomers oligomeric_state The Aβ25–28 loops of the six monomers within the asymmetric unit vary substantially in backbone geometry and side chain rotamers (Figures 2B and S1). RESULTS | |
| 4 20 electron density evidence The electron density for the loops is weak and diffuse compared to the electron density for the β-strands. RESULTS | |
| 29 34 loops structure_element The electron density for the loops is weak and diffuse compared to the electron density for the β-strands. RESULTS | |
| 71 87 electron density evidence The electron density for the loops is weak and diffuse compared to the electron density for the β-strands. RESULTS | |
| 96 105 β-strands structure_element The electron density for the loops is weak and diffuse compared to the electron density for the β-strands. RESULTS | |
| 4 12 B values evidence The B values for the loops are large, indicating that the loops are dynamic and not well ordered. RESULTS | |
| 21 26 loops structure_element The B values for the loops are large, indicating that the loops are dynamic and not well ordered. RESULTS | |
| 58 63 loops structure_element The B values for the loops are large, indicating that the loops are dynamic and not well ordered. RESULTS | |
| 77 82 loops structure_element Thus, the differences in backbone geometry and side chain rotamers among the loops are likely of little significance and should be interpreted with caution. RESULTS | |
| 0 9 Peptide 2 mutant Peptide 2 assembles into oligomers similar in morphology to those formed by peptide 1. RESULTS | |
| 25 34 oligomers oligomeric_state Peptide 2 assembles into oligomers similar in morphology to those formed by peptide 1. RESULTS | |
| 76 85 peptide 1 mutant Peptide 2 assembles into oligomers similar in morphology to those formed by peptide 1. RESULTS | |
| 5 14 peptide 1 mutant Like peptide 1, peptide 2 forms a triangular trimer, and four trimers assemble to form a dodecamer. RESULTS | |
| 16 25 peptide 2 mutant Like peptide 1, peptide 2 forms a triangular trimer, and four trimers assemble to form a dodecamer. RESULTS | |
| 34 44 triangular protein_state Like peptide 1, peptide 2 forms a triangular trimer, and four trimers assemble to form a dodecamer. RESULTS | |
| 45 51 trimer oligomeric_state Like peptide 1, peptide 2 forms a triangular trimer, and four trimers assemble to form a dodecamer. RESULTS | |
| 62 69 trimers oligomeric_state Like peptide 1, peptide 2 forms a triangular trimer, and four trimers assemble to form a dodecamer. RESULTS | |
| 89 98 dodecamer oligomeric_state Like peptide 1, peptide 2 forms a triangular trimer, and four trimers assemble to form a dodecamer. RESULTS | |
| 36 46 dodecamers oligomeric_state In the higher-order assembly of the dodecamers formed by peptide 2 a new structure emerges, not seen in peptide 1, an annular pore consisting of five dodecamers. RESULTS | |
| 57 66 peptide 2 mutant In the higher-order assembly of the dodecamers formed by peptide 2 a new structure emerges, not seen in peptide 1, an annular pore consisting of five dodecamers. RESULTS | |
| 73 82 structure evidence In the higher-order assembly of the dodecamers formed by peptide 2 a new structure emerges, not seen in peptide 1, an annular pore consisting of five dodecamers. RESULTS | |
| 104 113 peptide 1 mutant In the higher-order assembly of the dodecamers formed by peptide 2 a new structure emerges, not seen in peptide 1, an annular pore consisting of five dodecamers. RESULTS | |
| 118 130 annular pore site In the higher-order assembly of the dodecamers formed by peptide 2 a new structure emerges, not seen in peptide 1, an annular pore consisting of five dodecamers. RESULTS | |
| 150 160 dodecamers oligomeric_state In the higher-order assembly of the dodecamers formed by peptide 2 a new structure emerges, not seen in peptide 1, an annular pore consisting of five dodecamers. RESULTS | |
| 0 6 Trimer oligomeric_state Trimer RESULTS | |
| 0 9 Peptide 2 mutant Peptide 2 forms a trimer, much like that which we observed previously for peptide 1, in which three β-hairpins assemble to form an equilateral triangle (Figure 3A). RESULTS | |
| 18 24 trimer oligomeric_state Peptide 2 forms a trimer, much like that which we observed previously for peptide 1, in which three β-hairpins assemble to form an equilateral triangle (Figure 3A). RESULTS | |
| 74 83 peptide 1 mutant Peptide 2 forms a trimer, much like that which we observed previously for peptide 1, in which three β-hairpins assemble to form an equilateral triangle (Figure 3A). RESULTS | |
| 100 110 β-hairpins structure_element Peptide 2 forms a trimer, much like that which we observed previously for peptide 1, in which three β-hairpins assemble to form an equilateral triangle (Figure 3A). RESULTS | |
| 131 151 equilateral triangle structure_element Peptide 2 forms a trimer, much like that which we observed previously for peptide 1, in which three β-hairpins assemble to form an equilateral triangle (Figure 3A). RESULTS | |
| 4 10 trimer oligomeric_state The trimer maintains all of the same stabilizing contacts as those of peptide 1. RESULTS | |
| 70 79 peptide 1 mutant The trimer maintains all of the same stabilizing contacts as those of peptide 1. RESULTS | |
| 0 16 Hydrogen bonding bond_interaction Hydrogen bonding and hydrophobic interactions between residues on the β-strands comprising Aβ17–23 and Aβ30–36 stabilize the core of the trimer. RESULTS | |
| 21 45 hydrophobic interactions bond_interaction Hydrogen bonding and hydrophobic interactions between residues on the β-strands comprising Aβ17–23 and Aβ30–36 stabilize the core of the trimer. RESULTS | |
| 70 79 β-strands structure_element Hydrogen bonding and hydrophobic interactions between residues on the β-strands comprising Aβ17–23 and Aβ30–36 stabilize the core of the trimer. RESULTS | |
| 91 93 Aβ protein Hydrogen bonding and hydrophobic interactions between residues on the β-strands comprising Aβ17–23 and Aβ30–36 stabilize the core of the trimer. RESULTS | |
| 93 98 17–23 residue_range Hydrogen bonding and hydrophobic interactions between residues on the β-strands comprising Aβ17–23 and Aβ30–36 stabilize the core of the trimer. RESULTS | |
| 103 105 Aβ protein Hydrogen bonding and hydrophobic interactions between residues on the β-strands comprising Aβ17–23 and Aβ30–36 stabilize the core of the trimer. RESULTS | |
| 105 110 30–36 residue_range Hydrogen bonding and hydrophobic interactions between residues on the β-strands comprising Aβ17–23 and Aβ30–36 stabilize the core of the trimer. RESULTS | |
| 125 129 core structure_element Hydrogen bonding and hydrophobic interactions between residues on the β-strands comprising Aβ17–23 and Aβ30–36 stabilize the core of the trimer. RESULTS | |
| 137 143 trimer oligomeric_state Hydrogen bonding and hydrophobic interactions between residues on the β-strands comprising Aβ17–23 and Aβ30–36 stabilize the core of the trimer. RESULTS | |
| 4 19 disulfide bonds ptm The disulfide bonds between residues 24 and 29 are adjacent to the structural core of the trimer and do not make any substantial intermolecular contacts. RESULTS | |
| 37 39 24 residue_number The disulfide bonds between residues 24 and 29 are adjacent to the structural core of the trimer and do not make any substantial intermolecular contacts. RESULTS | |
| 44 46 29 residue_number The disulfide bonds between residues 24 and 29 are adjacent to the structural core of the trimer and do not make any substantial intermolecular contacts. RESULTS | |
| 67 82 structural core structure_element The disulfide bonds between residues 24 and 29 are adjacent to the structural core of the trimer and do not make any substantial intermolecular contacts. RESULTS | |
| 90 96 trimer oligomeric_state The disulfide bonds between residues 24 and 29 are adjacent to the structural core of the trimer and do not make any substantial intermolecular contacts. RESULTS | |
| 34 41 trimers oligomeric_state Two crystallographically distinct trimers comprise the peptide portion of the asymmetric unit. RESULTS | |
| 55 62 peptide chemical Two crystallographically distinct trimers comprise the peptide portion of the asymmetric unit. RESULTS | |
| 8 15 trimers oligomeric_state The two trimers are almost identical in structure, differing slightly among side chain rotamers and loop conformations. RESULTS | |
| 100 104 loop structure_element The two trimers are almost identical in structure, differing slightly among side chain rotamers and loop conformations. RESULTS | |
| 0 32 X-ray crystallographic structure evidence X-ray crystallographic structure of the trimer formed by peptide 2. (A) Triangular trimer. FIG | |
| 40 46 trimer oligomeric_state X-ray crystallographic structure of the trimer formed by peptide 2. (A) Triangular trimer. FIG | |
| 57 66 peptide 2 mutant X-ray crystallographic structure of the trimer formed by peptide 2. (A) Triangular trimer. FIG | |
| 72 82 Triangular protein_state X-ray crystallographic structure of the trimer formed by peptide 2. (A) Triangular trimer. FIG | |
| 83 89 trimer oligomeric_state X-ray crystallographic structure of the trimer formed by peptide 2. (A) Triangular trimer. FIG | |
| 10 15 water chemical The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 52 58 trimer oligomeric_state The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 121 135 hydrogen bonds bond_interaction The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 163 166 V18 residue_name_number The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 171 174 E22 residue_name_number The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 179 183 δOrn structure_element The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 188 191 C24 residue_name_number The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 221 231 triangular protein_state The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 232 238 trimer oligomeric_state The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 248 251 F19 residue_name_number The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 264 270 trimer oligomeric_state The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 319 322 F20 residue_name_number The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 335 341 trimer oligomeric_state The three water molecules in the center hole of the trimer are shown as spheres. (B) Detailed view of the intermolecular hydrogen bonds between the main chains of V18 and E22 and δOrn and C24, at the three corners of the triangular trimer. (C) The F19 face of the trimer, with key side chains shown as spheres. (D) The F20 face of the trimer, with key side chains as spheres. FIG | |
| 31 45 hydrogen bonds bond_interaction A network of 18 intermolecular hydrogen bonds helps stabilize the trimer. RESULTS | |
| 66 72 trimer oligomeric_state A network of 18 intermolecular hydrogen bonds helps stabilize the trimer. RESULTS | |
| 22 28 trimer oligomeric_state At the corners of the trimer, the pairs of β-hairpin monomers form four hydrogen bonds: two between the main chains of V18 and E22 and two between δOrn and the main chain of C24 (Figure 3B). RESULTS | |
| 43 52 β-hairpin structure_element At the corners of the trimer, the pairs of β-hairpin monomers form four hydrogen bonds: two between the main chains of V18 and E22 and two between δOrn and the main chain of C24 (Figure 3B). RESULTS | |
| 53 61 monomers oligomeric_state At the corners of the trimer, the pairs of β-hairpin monomers form four hydrogen bonds: two between the main chains of V18 and E22 and two between δOrn and the main chain of C24 (Figure 3B). RESULTS | |
| 72 86 hydrogen bonds bond_interaction At the corners of the trimer, the pairs of β-hairpin monomers form four hydrogen bonds: two between the main chains of V18 and E22 and two between δOrn and the main chain of C24 (Figure 3B). RESULTS | |
| 119 122 V18 residue_name_number At the corners of the trimer, the pairs of β-hairpin monomers form four hydrogen bonds: two between the main chains of V18 and E22 and two between δOrn and the main chain of C24 (Figure 3B). RESULTS | |
| 127 130 E22 residue_name_number At the corners of the trimer, the pairs of β-hairpin monomers form four hydrogen bonds: two between the main chains of V18 and E22 and two between δOrn and the main chain of C24 (Figure 3B). RESULTS | |
| 147 151 δOrn structure_element At the corners of the trimer, the pairs of β-hairpin monomers form four hydrogen bonds: two between the main chains of V18 and E22 and two between δOrn and the main chain of C24 (Figure 3B). RESULTS | |
| 174 177 C24 residue_name_number At the corners of the trimer, the pairs of β-hairpin monomers form four hydrogen bonds: two between the main chains of V18 and E22 and two between δOrn and the main chain of C24 (Figure 3B). RESULTS | |
| 14 19 water chemical Three ordered water molecules fill the hole in the center of the trimer, hydrogen bonding to each other and to the main chain of F20 (Figure 3A). RESULTS | |
| 65 71 trimer oligomeric_state Three ordered water molecules fill the hole in the center of the trimer, hydrogen bonding to each other and to the main chain of F20 (Figure 3A). RESULTS | |
| 73 89 hydrogen bonding bond_interaction Three ordered water molecules fill the hole in the center of the trimer, hydrogen bonding to each other and to the main chain of F20 (Figure 3A). RESULTS | |
| 129 132 F20 residue_name_number Three ordered water molecules fill the hole in the center of the trimer, hydrogen bonding to each other and to the main chain of F20 (Figure 3A). RESULTS | |
| 0 20 Hydrophobic contacts bond_interaction Hydrophobic contacts between residues at the three corners of the trimer, where the β-hairpins meet, further stabilize the trimer. RESULTS | |
| 66 72 trimer oligomeric_state Hydrophobic contacts between residues at the three corners of the trimer, where the β-hairpins meet, further stabilize the trimer. RESULTS | |
| 84 94 β-hairpins structure_element Hydrophobic contacts between residues at the three corners of the trimer, where the β-hairpins meet, further stabilize the trimer. RESULTS | |
| 123 129 trimer oligomeric_state Hydrophobic contacts between residues at the three corners of the trimer, where the β-hairpins meet, further stabilize the trimer. RESULTS | |
| 44 47 L17 residue_name_number At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 49 52 F19 residue_name_number At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 58 61 V36 residue_name_number At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 69 78 β-hairpin structure_element At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 120 123 A21 residue_name_number At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 125 128 I32 residue_name_number At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 130 133 L34 residue_name_number At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 144 147 D23 residue_name_number At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 164 173 β-hairpin structure_element At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 186 205 hydrophobic cluster site At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 229 249 hydrophobic clusters site At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 265 284 hydrophobic surface site At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 304 310 trimer oligomeric_state At each corner, the side chains of residues L17, F19, and V36 of one β-hairpin pack against the side chains of residues A21, I32, L34, and also D23 of the adjacent β-hairpin to create a hydrophobic cluster (Figure 3C). The three hydrophobic clusters create a large hydrophobic surface on one face of the trimer. RESULTS | |
| 22 28 trimer oligomeric_state The other face of the trimer displays a smaller hydrophobic surface, which includes the side chains of residues V18, F20, and I31 of the three β-hairpins (Figure 3D). RESULTS | |
| 48 67 hydrophobic surface site The other face of the trimer displays a smaller hydrophobic surface, which includes the side chains of residues V18, F20, and I31 of the three β-hairpins (Figure 3D). RESULTS | |
| 112 115 V18 residue_name_number The other face of the trimer displays a smaller hydrophobic surface, which includes the side chains of residues V18, F20, and I31 of the three β-hairpins (Figure 3D). RESULTS | |
| 117 120 F20 residue_name_number The other face of the trimer displays a smaller hydrophobic surface, which includes the side chains of residues V18, F20, and I31 of the three β-hairpins (Figure 3D). RESULTS | |
| 126 129 I31 residue_name_number The other face of the trimer displays a smaller hydrophobic surface, which includes the side chains of residues V18, F20, and I31 of the three β-hairpins (Figure 3D). RESULTS | |
| 143 153 β-hairpins structure_element The other face of the trimer displays a smaller hydrophobic surface, which includes the side chains of residues V18, F20, and I31 of the three β-hairpins (Figure 3D). RESULTS | |
| 63 66 F19 residue_name_number In subsequent discussion, we designate the former surface the “F19 face” and the latter surface the “F20 face”. RESULTS | |
| 101 104 F20 residue_name_number In subsequent discussion, we designate the former surface the “F19 face” and the latter surface the “F20 face”. RESULTS | |
| 0 9 Dodecamer oligomeric_state Dodecamer RESULTS | |
| 5 12 trimers oligomeric_state Four trimers assemble to form a dodecamer. RESULTS | |
| 32 41 dodecamer oligomeric_state Four trimers assemble to form a dodecamer. RESULTS | |
| 9 16 trimers oligomeric_state The four trimers arrange in a tetrahedral fashion, creating a central cavity inside the dodecamer. Because each trimer is triangular, the resulting arrangement resembles an octahedron. RESULTS | |
| 30 41 tetrahedral protein_state The four trimers arrange in a tetrahedral fashion, creating a central cavity inside the dodecamer. Because each trimer is triangular, the resulting arrangement resembles an octahedron. RESULTS | |
| 62 76 central cavity site The four trimers arrange in a tetrahedral fashion, creating a central cavity inside the dodecamer. Because each trimer is triangular, the resulting arrangement resembles an octahedron. RESULTS | |
| 88 97 dodecamer oligomeric_state The four trimers arrange in a tetrahedral fashion, creating a central cavity inside the dodecamer. Because each trimer is triangular, the resulting arrangement resembles an octahedron. RESULTS | |
| 112 118 trimer oligomeric_state The four trimers arrange in a tetrahedral fashion, creating a central cavity inside the dodecamer. Because each trimer is triangular, the resulting arrangement resembles an octahedron. RESULTS | |
| 122 132 triangular protein_state The four trimers arrange in a tetrahedral fashion, creating a central cavity inside the dodecamer. Because each trimer is triangular, the resulting arrangement resembles an octahedron. RESULTS | |
| 173 183 octahedron protein_state The four trimers arrange in a tetrahedral fashion, creating a central cavity inside the dodecamer. Because each trimer is triangular, the resulting arrangement resembles an octahedron. RESULTS | |
| 15 25 β-hairpins structure_element Each of the 12 β-hairpins constitutes an edge of the octahedron, and the triangular trimers occupy four of the eight faces of the octahedron. RESULTS | |
| 53 63 octahedron protein_state Each of the 12 β-hairpins constitutes an edge of the octahedron, and the triangular trimers occupy four of the eight faces of the octahedron. RESULTS | |
| 73 83 triangular protein_state Each of the 12 β-hairpins constitutes an edge of the octahedron, and the triangular trimers occupy four of the eight faces of the octahedron. RESULTS | |
| 84 91 trimers oligomeric_state Each of the 12 β-hairpins constitutes an edge of the octahedron, and the triangular trimers occupy four of the eight faces of the octahedron. RESULTS | |
| 130 140 octahedron protein_state Each of the 12 β-hairpins constitutes an edge of the octahedron, and the triangular trimers occupy four of the eight faces of the octahedron. RESULTS | |
| 26 36 octahedral protein_state Figure 4A illustrates the octahedral shape of the dodecamer. RESULTS | |
| 50 59 dodecamer oligomeric_state Figure 4A illustrates the octahedral shape of the dodecamer. RESULTS | |
| 26 37 tetrahedral protein_state Figure 4B illustrates the tetrahedral arrangement of the four trimers. RESULTS | |
| 62 69 trimers oligomeric_state Figure 4B illustrates the tetrahedral arrangement of the four trimers. RESULTS | |
| 40 49 dodecamer oligomeric_state X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 60 69 peptide 2 mutant X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 87 96 dodecamer oligomeric_state X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 118 128 octahedral protein_state X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 152 161 dodecamer oligomeric_state X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 183 194 tetrahedral protein_state X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 219 226 trimers oligomeric_state X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 245 254 dodecamer oligomeric_state X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 272 278 trimer oligomeric_state X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 279 287 subunits structure_element X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 304 310 cavity site X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 318 327 dodecamer oligomeric_state X-ray crystallographic structure of the dodecamer formed by peptide 2. (A) View of the dodecamer that illustrates the octahedral shape. (B) View of the dodecamer that illustrates the tetrahedral arrangement of the four trimers that comprise the dodecamer. (C) View of two trimer subunits from inside the cavity of the dodecamer. FIG | |
| 9 12 L17 residue_name_number Residues L17, L34, and V36 are shown as spheres, illustrating the hydrophobic packing that occurs at the six vertices of the dodecamer. (D) Detailed view of one of the six vertices of the dodecamer. FIG | |
| 14 17 L34 residue_name_number Residues L17, L34, and V36 are shown as spheres, illustrating the hydrophobic packing that occurs at the six vertices of the dodecamer. (D) Detailed view of one of the six vertices of the dodecamer. FIG | |
| 23 26 V36 residue_name_number Residues L17, L34, and V36 are shown as spheres, illustrating the hydrophobic packing that occurs at the six vertices of the dodecamer. (D) Detailed view of one of the six vertices of the dodecamer. FIG | |
| 66 85 hydrophobic packing bond_interaction Residues L17, L34, and V36 are shown as spheres, illustrating the hydrophobic packing that occurs at the six vertices of the dodecamer. (D) Detailed view of one of the six vertices of the dodecamer. FIG | |
| 125 134 dodecamer oligomeric_state Residues L17, L34, and V36 are shown as spheres, illustrating the hydrophobic packing that occurs at the six vertices of the dodecamer. (D) Detailed view of one of the six vertices of the dodecamer. FIG | |
| 188 197 dodecamer oligomeric_state Residues L17, L34, and V36 are shown as spheres, illustrating the hydrophobic packing that occurs at the six vertices of the dodecamer. (D) Detailed view of one of the six vertices of the dodecamer. FIG | |
| 4 7 F19 residue_name_number The F19 faces of the trimers line the interior of the dodecamer. RESULTS | |
| 21 28 trimers oligomeric_state The F19 faces of the trimers line the interior of the dodecamer. RESULTS | |
| 54 63 dodecamer oligomeric_state The F19 faces of the trimers line the interior of the dodecamer. RESULTS | |
| 21 40 hydrophobic packing bond_interaction At the six vertices, hydrophobic packing between the side chains of L17, L34, and V36 helps stabilize the dodecamer (Figures 4C and D). RESULTS | |
| 68 71 L17 residue_name_number At the six vertices, hydrophobic packing between the side chains of L17, L34, and V36 helps stabilize the dodecamer (Figures 4C and D). RESULTS | |
| 73 76 L34 residue_name_number At the six vertices, hydrophobic packing between the side chains of L17, L34, and V36 helps stabilize the dodecamer (Figures 4C and D). RESULTS | |
| 82 85 V36 residue_name_number At the six vertices, hydrophobic packing between the side chains of L17, L34, and V36 helps stabilize the dodecamer (Figures 4C and D). RESULTS | |
| 106 115 dodecamer oligomeric_state At the six vertices, hydrophobic packing between the side chains of L17, L34, and V36 helps stabilize the dodecamer (Figures 4C and D). RESULTS | |
| 40 43 D23 residue_name_number Salt bridges between the side chains of D23 and δOrn at the vertices further stabilize the dodecamer. RESULTS | |
| 48 52 δOrn structure_element Salt bridges between the side chains of D23 and δOrn at the vertices further stabilize the dodecamer. RESULTS | |
| 91 100 dodecamer oligomeric_state Salt bridges between the side chains of D23 and δOrn at the vertices further stabilize the dodecamer. RESULTS | |
| 38 40 Aβ protein Each of the six vertices includes two Aβ25–28 loops that extend past the core of the dodecamer without making any substantial intermolecular contacts. RESULTS | |
| 40 45 25–28 residue_range Each of the six vertices includes two Aβ25–28 loops that extend past the core of the dodecamer without making any substantial intermolecular contacts. RESULTS | |
| 46 51 loops structure_element Each of the six vertices includes two Aβ25–28 loops that extend past the core of the dodecamer without making any substantial intermolecular contacts. RESULTS | |
| 73 77 core structure_element Each of the six vertices includes two Aβ25–28 loops that extend past the core of the dodecamer without making any substantial intermolecular contacts. RESULTS | |
| 85 94 dodecamer oligomeric_state Each of the six vertices includes two Aβ25–28 loops that extend past the core of the dodecamer without making any substantial intermolecular contacts. RESULTS | |
| 20 29 dodecamer oligomeric_state The exterior of the dodecamer displays four F20 faces (Figure S3). RESULTS | |
| 44 47 F20 residue_name_number The exterior of the dodecamer displays four F20 faces (Figure S3). RESULTS | |
| 7 22 crystal lattice evidence In the crystal lattice, each F20 face of one dodecamer packs against an F20 face of another dodecamer. RESULTS | |
| 29 32 F20 residue_name_number In the crystal lattice, each F20 face of one dodecamer packs against an F20 face of another dodecamer. RESULTS | |
| 45 54 dodecamer oligomeric_state In the crystal lattice, each F20 face of one dodecamer packs against an F20 face of another dodecamer. RESULTS | |
| 72 75 F20 residue_name_number In the crystal lattice, each F20 face of one dodecamer packs against an F20 face of another dodecamer. RESULTS | |
| 92 101 dodecamer oligomeric_state In the crystal lattice, each F20 face of one dodecamer packs against an F20 face of another dodecamer. RESULTS | |
| 46 55 dodecamer oligomeric_state Although the asymmetric unit comprises half a dodecamer, the crystal lattice may be thought of as being built of dodecamers. RESULTS | |
| 61 76 crystal lattice evidence Although the asymmetric unit comprises half a dodecamer, the crystal lattice may be thought of as being built of dodecamers. RESULTS | |
| 113 123 dodecamers oligomeric_state Although the asymmetric unit comprises half a dodecamer, the crystal lattice may be thought of as being built of dodecamers. RESULTS | |
| 4 24 electron density map evidence The electron density map for the X-ray crystallographic structure of peptide 2 has long tubes of electron density inside the central cavity of the dodecamer. RESULTS | |
| 33 65 X-ray crystallographic structure evidence The electron density map for the X-ray crystallographic structure of peptide 2 has long tubes of electron density inside the central cavity of the dodecamer. RESULTS | |
| 69 78 peptide 2 mutant The electron density map for the X-ray crystallographic structure of peptide 2 has long tubes of electron density inside the central cavity of the dodecamer. RESULTS | |
| 97 113 electron density evidence The electron density map for the X-ray crystallographic structure of peptide 2 has long tubes of electron density inside the central cavity of the dodecamer. RESULTS | |
| 125 139 central cavity site The electron density map for the X-ray crystallographic structure of peptide 2 has long tubes of electron density inside the central cavity of the dodecamer. RESULTS | |
| 147 156 dodecamer oligomeric_state The electron density map for the X-ray crystallographic structure of peptide 2 has long tubes of electron density inside the central cavity of the dodecamer. RESULTS | |
| 28 44 electron density evidence The shape and length of the electron density is consistent with the structure of Jeffamine M-600, which is an essential component of the crystallization conditions. RESULTS | |
| 68 77 structure evidence The shape and length of the electron density is consistent with the structure of Jeffamine M-600, which is an essential component of the crystallization conditions. RESULTS | |
| 81 96 Jeffamine M-600 chemical The shape and length of the electron density is consistent with the structure of Jeffamine M-600, which is an essential component of the crystallization conditions. RESULTS | |
| 0 15 Jeffamine M-600 chemical Jeffamine M-600 is a polypropylene glycol derivative with a 2-methoxyethoxy unit at one end and a 2-aminopropyl unit at the other end. RESULTS | |
| 9 24 Jeffamine M-600 chemical Although Jeffamine M-600 is a heterogeneous mixture with varying chain lengths and stereochemistry, we modeled a single stereoisomer with nine propylene glycol units (n = 9) to fit the electron density. RESULTS | |
| 185 201 electron density evidence Although Jeffamine M-600 is a heterogeneous mixture with varying chain lengths and stereochemistry, we modeled a single stereoisomer with nine propylene glycol units (n = 9) to fit the electron density. RESULTS | |
| 4 19 Jeffamine M-600 chemical The Jeffamine M-600 appears to stabilize the dodecamer by occupying the central cavity and making hydrophobic contacts with residues lining the cavity (Figure S3). RESULTS | |
| 45 54 dodecamer oligomeric_state The Jeffamine M-600 appears to stabilize the dodecamer by occupying the central cavity and making hydrophobic contacts with residues lining the cavity (Figure S3). RESULTS | |
| 72 86 central cavity site The Jeffamine M-600 appears to stabilize the dodecamer by occupying the central cavity and making hydrophobic contacts with residues lining the cavity (Figure S3). RESULTS | |
| 98 118 hydrophobic contacts bond_interaction The Jeffamine M-600 appears to stabilize the dodecamer by occupying the central cavity and making hydrophobic contacts with residues lining the cavity (Figure S3). RESULTS | |
| 144 150 cavity site The Jeffamine M-600 appears to stabilize the dodecamer by occupying the central cavity and making hydrophobic contacts with residues lining the cavity (Figure S3). RESULTS | |
| 5 14 dodecamer oligomeric_state In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 25 36 full-length protein_state In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 37 39 Aβ protein In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 78 80 Aβ protein In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 80 85 37–40 residue_range In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 89 91 Aβ protein In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 91 96 37–42 residue_range In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 139 148 dodecamer oligomeric_state In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 174 190 hydrophobic core site In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 202 216 central cavity site In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 224 233 dodecamer oligomeric_state In a dodecamer formed by full-length Aβ, the hydrophobic C-terminal residues (Aβ37–40 or Aβ37–42) might play a similar role in filling the dodecamer and thus create a packed hydrophobic core within the central cavity of the dodecamer. RESULTS | |
| 0 12 Annular Pore site Annular Pore RESULTS | |
| 5 15 dodecamers oligomeric_state Five dodecamers assemble to form an annular porelike structure (Figure 5A). RESULTS | |
| 44 52 porelike structure_element Five dodecamers assemble to form an annular porelike structure (Figure 5A). RESULTS | |
| 0 19 Hydrophobic packing bond_interaction Hydrophobic packing between the F20 faces of trimers displayed on the outer surface of each dodecamer stabilizes the porelike assembly. RESULTS | |
| 32 35 F20 residue_name_number Hydrophobic packing between the F20 faces of trimers displayed on the outer surface of each dodecamer stabilizes the porelike assembly. RESULTS | |
| 45 52 trimers oligomeric_state Hydrophobic packing between the F20 faces of trimers displayed on the outer surface of each dodecamer stabilizes the porelike assembly. RESULTS | |
| 92 101 dodecamer oligomeric_state Hydrophobic packing between the F20 faces of trimers displayed on the outer surface of each dodecamer stabilizes the porelike assembly. RESULTS | |
| 50 57 trimers oligomeric_state Two morphologically distinct interactions between trimers occur at the interfaces of the five dodecamers: one in which the trimers are eclipsed (Figure 5B), and one in which the trimers are staggered (Figure 5C). RESULTS | |
| 71 81 interfaces site Two morphologically distinct interactions between trimers occur at the interfaces of the five dodecamers: one in which the trimers are eclipsed (Figure 5B), and one in which the trimers are staggered (Figure 5C). RESULTS | |
| 94 104 dodecamers oligomeric_state Two morphologically distinct interactions between trimers occur at the interfaces of the five dodecamers: one in which the trimers are eclipsed (Figure 5B), and one in which the trimers are staggered (Figure 5C). RESULTS | |
| 123 130 trimers oligomeric_state Two morphologically distinct interactions between trimers occur at the interfaces of the five dodecamers: one in which the trimers are eclipsed (Figure 5B), and one in which the trimers are staggered (Figure 5C). RESULTS | |
| 135 143 eclipsed protein_state Two morphologically distinct interactions between trimers occur at the interfaces of the five dodecamers: one in which the trimers are eclipsed (Figure 5B), and one in which the trimers are staggered (Figure 5C). RESULTS | |
| 178 185 trimers oligomeric_state Two morphologically distinct interactions between trimers occur at the interfaces of the five dodecamers: one in which the trimers are eclipsed (Figure 5B), and one in which the trimers are staggered (Figure 5C). RESULTS | |
| 190 199 staggered protein_state Two morphologically distinct interactions between trimers occur at the interfaces of the five dodecamers: one in which the trimers are eclipsed (Figure 5B), and one in which the trimers are staggered (Figure 5C). RESULTS | |
| 0 19 Hydrophobic packing bond_interaction Hydrophobic packing between the side chains of F20, I31, and E22 stabilizes these interfaces (Figure 5D and E). RESULTS | |
| 47 50 F20 residue_name_number Hydrophobic packing between the side chains of F20, I31, and E22 stabilizes these interfaces (Figure 5D and E). RESULTS | |
| 52 55 I31 residue_name_number Hydrophobic packing between the side chains of F20, I31, and E22 stabilizes these interfaces (Figure 5D and E). RESULTS | |
| 61 64 E22 residue_name_number Hydrophobic packing between the side chains of F20, I31, and E22 stabilizes these interfaces (Figure 5D and E). RESULTS | |
| 82 92 interfaces site Hydrophobic packing between the side chains of F20, I31, and E22 stabilizes these interfaces (Figure 5D and E). RESULTS | |
| 4 16 annular pore site The annular pore contains three eclipsed interfaces and two staggered interfaces. RESULTS | |
| 32 40 eclipsed protein_state The annular pore contains three eclipsed interfaces and two staggered interfaces. RESULTS | |
| 41 51 interfaces site The annular pore contains three eclipsed interfaces and two staggered interfaces. RESULTS | |
| 60 69 staggered protein_state The annular pore contains three eclipsed interfaces and two staggered interfaces. RESULTS | |
| 70 80 interfaces site The annular pore contains three eclipsed interfaces and two staggered interfaces. RESULTS | |
| 4 12 eclipsed protein_state The eclipsed interfaces occur between dodecamers 1 and 2, 1 and 5, and 3 and 4, as shown in Figure 5A. RESULTS | |
| 13 23 interfaces site The eclipsed interfaces occur between dodecamers 1 and 2, 1 and 5, and 3 and 4, as shown in Figure 5A. RESULTS | |
| 38 56 dodecamers 1 and 2 structure_element The eclipsed interfaces occur between dodecamers 1 and 2, 1 and 5, and 3 and 4, as shown in Figure 5A. RESULTS | |
| 58 65 1 and 5 structure_element The eclipsed interfaces occur between dodecamers 1 and 2, 1 and 5, and 3 and 4, as shown in Figure 5A. RESULTS | |
| 71 78 3 and 4 structure_element The eclipsed interfaces occur between dodecamers 1 and 2, 1 and 5, and 3 and 4, as shown in Figure 5A. RESULTS | |
| 4 13 staggered protein_state The staggered interfaces occur between dodecamers 2 and 3 and 4 and 5. RESULTS | |
| 14 24 interfaces site The staggered interfaces occur between dodecamers 2 and 3 and 4 and 5. RESULTS | |
| 39 57 dodecamers 2 and 3 structure_element The staggered interfaces occur between dodecamers 2 and 3 and 4 and 5. RESULTS | |
| 62 69 4 and 5 structure_element The staggered interfaces occur between dodecamers 2 and 3 and 4 and 5. RESULTS | |
| 4 16 annular pore site The annular pore is not completely flat, instead, adopting a slightly puckered shape, which accommodates the eclipsed and staggered interfaces. RESULTS | |
| 109 117 eclipsed protein_state The annular pore is not completely flat, instead, adopting a slightly puckered shape, which accommodates the eclipsed and staggered interfaces. RESULTS | |
| 122 131 staggered protein_state The annular pore is not completely flat, instead, adopting a slightly puckered shape, which accommodates the eclipsed and staggered interfaces. RESULTS | |
| 132 142 interfaces site The annular pore is not completely flat, instead, adopting a slightly puckered shape, which accommodates the eclipsed and staggered interfaces. RESULTS | |
| 4 6 Aβ protein Ten Aβ25–28 loops from the vertices of the five dodecamers line the hole in the center of the pore. RESULTS | |
| 6 11 25–28 residue_range Ten Aβ25–28 loops from the vertices of the five dodecamers line the hole in the center of the pore. RESULTS | |
| 12 17 loops structure_element Ten Aβ25–28 loops from the vertices of the five dodecamers line the hole in the center of the pore. RESULTS | |
| 48 58 dodecamers oligomeric_state Ten Aβ25–28 loops from the vertices of the five dodecamers line the hole in the center of the pore. RESULTS | |
| 94 98 pore site Ten Aβ25–28 loops from the vertices of the five dodecamers line the hole in the center of the pore. RESULTS | |
| 31 34 S26 residue_name_number The hydrophilic side chains of S26, N27, and K28 decorate the hole. RESULTS | |
| 36 39 N27 residue_name_number The hydrophilic side chains of S26, N27, and K28 decorate the hole. RESULTS | |
| 45 48 K28 residue_name_number The hydrophilic side chains of S26, N27, and K28 decorate the hole. RESULTS | |
| 0 32 X-ray crystallographic structure evidence X-ray crystallographic structure of the annular pore formed by peptide 2. (A) Annular porelike structure illustrating the relationship of the five dodecamers that form the pore (top view). FIG | |
| 40 52 annular pore site X-ray crystallographic structure of the annular pore formed by peptide 2. (A) Annular porelike structure illustrating the relationship of the five dodecamers that form the pore (top view). FIG | |
| 63 72 peptide 2 mutant X-ray crystallographic structure of the annular pore formed by peptide 2. (A) Annular porelike structure illustrating the relationship of the five dodecamers that form the pore (top view). FIG | |
| 78 94 Annular porelike structure_element X-ray crystallographic structure of the annular pore formed by peptide 2. (A) Annular porelike structure illustrating the relationship of the five dodecamers that form the pore (top view). FIG | |
| 95 104 structure evidence X-ray crystallographic structure of the annular pore formed by peptide 2. (A) Annular porelike structure illustrating the relationship of the five dodecamers that form the pore (top view). FIG | |
| 147 157 dodecamers oligomeric_state X-ray crystallographic structure of the annular pore formed by peptide 2. (A) Annular porelike structure illustrating the relationship of the five dodecamers that form the pore (top view). FIG | |
| 172 176 pore site X-ray crystallographic structure of the annular pore formed by peptide 2. (A) Annular porelike structure illustrating the relationship of the five dodecamers that form the pore (top view). FIG | |
| 5 23 Eclipsed interface site (B) Eclipsed interface between dodecamers 1 and 2 (side view). FIG | |
| 32 50 dodecamers 1 and 2 structure_element (B) Eclipsed interface between dodecamers 1 and 2 (side view). FIG | |
| 9 27 eclipsed interface site The same eclipsed interface also occurs between dodecamers 1 and 5 and 3 and 4. (C) Staggered interface between dodecamers 2 and 3 (side view). FIG | |
| 48 66 dodecamers 1 and 5 structure_element The same eclipsed interface also occurs between dodecamers 1 and 5 and 3 and 4. (C) Staggered interface between dodecamers 2 and 3 (side view). FIG | |
| 71 78 3 and 4 structure_element The same eclipsed interface also occurs between dodecamers 1 and 5 and 3 and 4. (C) Staggered interface between dodecamers 2 and 3 (side view). FIG | |
| 84 103 Staggered interface site The same eclipsed interface also occurs between dodecamers 1 and 5 and 3 and 4. (C) Staggered interface between dodecamers 2 and 3 (side view). FIG | |
| 112 130 dodecamers 2 and 3 structure_element The same eclipsed interface also occurs between dodecamers 1 and 5 and 3 and 4. (C) Staggered interface between dodecamers 2 and 3 (side view). FIG | |
| 9 28 staggered interface site The same staggered interface also occurs between dodecamers 4 and 5. (D) Eclipsed interface between dodecamers 1 and 5 (top view). FIG | |
| 73 91 Eclipsed interface site The same staggered interface also occurs between dodecamers 4 and 5. (D) Eclipsed interface between dodecamers 1 and 5 (top view). FIG | |
| 100 118 dodecamers 1 and 5 structure_element The same staggered interface also occurs between dodecamers 4 and 5. (D) Eclipsed interface between dodecamers 1 and 5 (top view). FIG | |
| 4 16 annular pore site The annular pore is comparable in size to other large protein assemblies. RESULTS | |
| 46 50 pore site The diameter of the hole in the center of the pore is ∼2 nm. RESULTS | |
| 21 25 pore site The thickness of the pore is ∼5 nm, which is comparable to that of a lipid bilayer membrane. RESULTS | |
| 33 45 annular pore site It is important to note that the annular pore formed by peptide 2 is not a discrete unit in the crystal lattice. RESULTS | |
| 56 65 peptide 2 mutant It is important to note that the annular pore formed by peptide 2 is not a discrete unit in the crystal lattice. RESULTS | |
| 96 111 crystal lattice evidence It is important to note that the annular pore formed by peptide 2 is not a discrete unit in the crystal lattice. RESULTS | |
| 12 27 crystal lattice evidence Rather, the crystal lattice is composed of conjoined annular pores in which all four F20 faces on the surface of each dodecamer contact F20 faces on other dodecamers (Figure S4). RESULTS | |
| 53 66 annular pores site Rather, the crystal lattice is composed of conjoined annular pores in which all four F20 faces on the surface of each dodecamer contact F20 faces on other dodecamers (Figure S4). RESULTS | |
| 85 88 F20 residue_name_number Rather, the crystal lattice is composed of conjoined annular pores in which all four F20 faces on the surface of each dodecamer contact F20 faces on other dodecamers (Figure S4). RESULTS | |
| 118 127 dodecamer oligomeric_state Rather, the crystal lattice is composed of conjoined annular pores in which all four F20 faces on the surface of each dodecamer contact F20 faces on other dodecamers (Figure S4). RESULTS | |
| 136 139 F20 residue_name_number Rather, the crystal lattice is composed of conjoined annular pores in which all four F20 faces on the surface of each dodecamer contact F20 faces on other dodecamers (Figure S4). RESULTS | |
| 155 165 dodecamers oligomeric_state Rather, the crystal lattice is composed of conjoined annular pores in which all four F20 faces on the surface of each dodecamer contact F20 faces on other dodecamers (Figure S4). RESULTS | |
| 4 19 crystal lattice evidence The crystal lattice shows how the dodecamers can further assemble to form larger structures. RESULTS | |
| 34 44 dodecamers oligomeric_state The crystal lattice shows how the dodecamers can further assemble to form larger structures. RESULTS | |
| 5 14 dodecamer oligomeric_state Each dodecamer may be thought of as a tetravalent building block with the potential to assemble on all four faces to form higher-order supramolecular assemblies. RESULTS | |
| 4 32 X-ray crystallographic study experimental_method The X-ray crystallographic study of peptide 2 described here provides high-resolution structures of oligomers formed by an Aβ17–36 β-hairpin. DISCUSS | |
| 36 45 peptide 2 mutant The X-ray crystallographic study of peptide 2 described here provides high-resolution structures of oligomers formed by an Aβ17–36 β-hairpin. DISCUSS | |
| 86 96 structures evidence The X-ray crystallographic study of peptide 2 described here provides high-resolution structures of oligomers formed by an Aβ17–36 β-hairpin. DISCUSS | |
| 100 109 oligomers oligomeric_state The X-ray crystallographic study of peptide 2 described here provides high-resolution structures of oligomers formed by an Aβ17–36 β-hairpin. DISCUSS | |
| 123 125 Aβ protein The X-ray crystallographic study of peptide 2 described here provides high-resolution structures of oligomers formed by an Aβ17–36 β-hairpin. DISCUSS | |
| 125 130 17–36 residue_range The X-ray crystallographic study of peptide 2 described here provides high-resolution structures of oligomers formed by an Aβ17–36 β-hairpin. DISCUSS | |
| 131 140 β-hairpin structure_element The X-ray crystallographic study of peptide 2 described here provides high-resolution structures of oligomers formed by an Aβ17–36 β-hairpin. DISCUSS | |
| 4 29 crystallographic assembly evidence The crystallographic assembly of peptide 2 into a trimer, dodecamer, and annular pore provides a model for the assembly of the full-length Aβ peptide to form oligomers. DISCUSS | |
| 33 42 peptide 2 mutant The crystallographic assembly of peptide 2 into a trimer, dodecamer, and annular pore provides a model for the assembly of the full-length Aβ peptide to form oligomers. DISCUSS | |
| 50 56 trimer oligomeric_state The crystallographic assembly of peptide 2 into a trimer, dodecamer, and annular pore provides a model for the assembly of the full-length Aβ peptide to form oligomers. DISCUSS | |
| 58 67 dodecamer oligomeric_state The crystallographic assembly of peptide 2 into a trimer, dodecamer, and annular pore provides a model for the assembly of the full-length Aβ peptide to form oligomers. DISCUSS | |
| 73 85 annular pore site The crystallographic assembly of peptide 2 into a trimer, dodecamer, and annular pore provides a model for the assembly of the full-length Aβ peptide to form oligomers. DISCUSS | |
| 127 138 full-length protein_state The crystallographic assembly of peptide 2 into a trimer, dodecamer, and annular pore provides a model for the assembly of the full-length Aβ peptide to form oligomers. DISCUSS | |
| 139 141 Aβ protein The crystallographic assembly of peptide 2 into a trimer, dodecamer, and annular pore provides a model for the assembly of the full-length Aβ peptide to form oligomers. DISCUSS | |
| 158 167 oligomers oligomeric_state The crystallographic assembly of peptide 2 into a trimer, dodecamer, and annular pore provides a model for the assembly of the full-length Aβ peptide to form oligomers. DISCUSS | |
| 14 16 Aβ protein In this model Aβ folds to form a β-hairpin comprising the hydrophobic central and C-terminal regions. DISCUSS | |
| 33 42 β-hairpin structure_element In this model Aβ folds to form a β-hairpin comprising the hydrophobic central and C-terminal regions. DISCUSS | |
| 70 100 central and C-terminal regions structure_element In this model Aβ folds to form a β-hairpin comprising the hydrophobic central and C-terminal regions. DISCUSS | |
| 6 16 β-hairpins structure_element Three β-hairpins assemble to form a trimer, and four trimers assemble to form a dodecamer. DISCUSS | |
| 36 42 trimer oligomeric_state Three β-hairpins assemble to form a trimer, and four trimers assemble to form a dodecamer. DISCUSS | |
| 53 60 trimers oligomeric_state Three β-hairpins assemble to form a trimer, and four trimers assemble to form a dodecamer. DISCUSS | |
| 80 89 dodecamer oligomeric_state Three β-hairpins assemble to form a trimer, and four trimers assemble to form a dodecamer. DISCUSS | |
| 4 14 dodecamers oligomeric_state The dodecamers further assemble to form an annular pore (Figure 6). DISCUSS | |
| 43 55 annular pore site The dodecamers further assemble to form an annular pore (Figure 6). DISCUSS | |
| 42 44 Aβ protein Model for the hierarchical assembly of an Aβ β-hairpin into a trimer, dodecamer, and annular pore based on the crystallographic assembly of peptide 2. FIG | |
| 45 54 β-hairpin structure_element Model for the hierarchical assembly of an Aβ β-hairpin into a trimer, dodecamer, and annular pore based on the crystallographic assembly of peptide 2. FIG | |
| 62 68 trimer oligomeric_state Model for the hierarchical assembly of an Aβ β-hairpin into a trimer, dodecamer, and annular pore based on the crystallographic assembly of peptide 2. FIG | |
| 70 79 dodecamer oligomeric_state Model for the hierarchical assembly of an Aβ β-hairpin into a trimer, dodecamer, and annular pore based on the crystallographic assembly of peptide 2. FIG | |
| 85 97 annular pore site Model for the hierarchical assembly of an Aβ β-hairpin into a trimer, dodecamer, and annular pore based on the crystallographic assembly of peptide 2. FIG | |
| 140 149 peptide 2 mutant Model for the hierarchical assembly of an Aβ β-hairpin into a trimer, dodecamer, and annular pore based on the crystallographic assembly of peptide 2. FIG | |
| 0 9 Monomeric oligomeric_state Monomeric Aβ folds to form a β-hairpin in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. FIG | |
| 10 12 Aβ protein Monomeric Aβ folds to form a β-hairpin in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. FIG | |
| 29 38 β-hairpin structure_element Monomeric Aβ folds to form a β-hairpin in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. FIG | |
| 64 71 central structure_element Monomeric Aβ folds to form a β-hairpin in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. FIG | |
| 76 94 C-terminal regions structure_element Monomeric Aβ folds to form a β-hairpin in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. FIG | |
| 103 123 antiparallel β-sheet structure_element Monomeric Aβ folds to form a β-hairpin in which the hydrophobic central and C-terminal regions form an antiparallel β-sheet. FIG | |
| 6 15 β-hairpin structure_element Three β-hairpin monomers assemble to form a triangular trimer. FIG | |
| 16 24 monomers oligomeric_state Three β-hairpin monomers assemble to form a triangular trimer. FIG | |
| 44 54 triangular protein_state Three β-hairpin monomers assemble to form a triangular trimer. FIG | |
| 55 61 trimer oligomeric_state Three β-hairpin monomers assemble to form a triangular trimer. FIG | |
| 5 15 triangular protein_state Four triangular trimers assemble to form a dodecamer. FIG | |
| 16 23 trimers oligomeric_state Four triangular trimers assemble to form a dodecamer. FIG | |
| 43 52 dodecamer oligomeric_state Four triangular trimers assemble to form a dodecamer. FIG | |
| 5 15 dodecamers oligomeric_state Five dodecamers assemble to form an annular pore. FIG | |
| 36 48 annular pore site Five dodecamers assemble to form an annular pore. FIG | |
| 45 49 Aβ42 protein The molecular weights shown correspond to an Aβ42 monomer (∼4.5 kDa), an Aβ42 trimer (∼13.5 kDa), an Aβ42 dodecamer (∼54 kDa), and an Aβ42 annular pore composed of five dodecamers (∼270 kDa). FIG | |
| 50 57 monomer oligomeric_state The molecular weights shown correspond to an Aβ42 monomer (∼4.5 kDa), an Aβ42 trimer (∼13.5 kDa), an Aβ42 dodecamer (∼54 kDa), and an Aβ42 annular pore composed of five dodecamers (∼270 kDa). FIG | |
| 73 77 Aβ42 protein The molecular weights shown correspond to an Aβ42 monomer (∼4.5 kDa), an Aβ42 trimer (∼13.5 kDa), an Aβ42 dodecamer (∼54 kDa), and an Aβ42 annular pore composed of five dodecamers (∼270 kDa). FIG | |
| 78 84 trimer oligomeric_state The molecular weights shown correspond to an Aβ42 monomer (∼4.5 kDa), an Aβ42 trimer (∼13.5 kDa), an Aβ42 dodecamer (∼54 kDa), and an Aβ42 annular pore composed of five dodecamers (∼270 kDa). FIG | |
| 101 105 Aβ42 protein The molecular weights shown correspond to an Aβ42 monomer (∼4.5 kDa), an Aβ42 trimer (∼13.5 kDa), an Aβ42 dodecamer (∼54 kDa), and an Aβ42 annular pore composed of five dodecamers (∼270 kDa). FIG | |
| 106 115 dodecamer oligomeric_state The molecular weights shown correspond to an Aβ42 monomer (∼4.5 kDa), an Aβ42 trimer (∼13.5 kDa), an Aβ42 dodecamer (∼54 kDa), and an Aβ42 annular pore composed of five dodecamers (∼270 kDa). FIG | |
| 134 138 Aβ42 protein The molecular weights shown correspond to an Aβ42 monomer (∼4.5 kDa), an Aβ42 trimer (∼13.5 kDa), an Aβ42 dodecamer (∼54 kDa), and an Aβ42 annular pore composed of five dodecamers (∼270 kDa). FIG | |
| 139 151 annular pore site The molecular weights shown correspond to an Aβ42 monomer (∼4.5 kDa), an Aβ42 trimer (∼13.5 kDa), an Aβ42 dodecamer (∼54 kDa), and an Aβ42 annular pore composed of five dodecamers (∼270 kDa). FIG | |
| 169 179 dodecamers oligomeric_state The molecular weights shown correspond to an Aβ42 monomer (∼4.5 kDa), an Aβ42 trimer (∼13.5 kDa), an Aβ42 dodecamer (∼54 kDa), and an Aβ42 annular pore composed of five dodecamers (∼270 kDa). FIG | |
| 91 93 Aβ protein The model put forth in Figure 6 is consistent with the current understanding of endogenous Aβ oligomerization and explains at atomic resolution many key observations about Aβ oligomers. DISCUSS | |
| 172 174 Aβ protein The model put forth in Figure 6 is consistent with the current understanding of endogenous Aβ oligomerization and explains at atomic resolution many key observations about Aβ oligomers. DISCUSS | |
| 175 184 oligomers oligomeric_state The model put forth in Figure 6 is consistent with the current understanding of endogenous Aβ oligomerization and explains at atomic resolution many key observations about Aβ oligomers. DISCUSS | |
| 32 34 Aβ protein Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 35 44 oligomers oligomeric_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 65 67 Aβ protein Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 68 77 oligomers oligomeric_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 105 112 fibrils oligomeric_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 118 127 fibrillar protein_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 128 137 oligomers oligomeric_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 144 146 Aβ protein Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 147 156 oligomers oligomeric_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 170 179 fibrillar protein_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 190 202 nonfibrillar protein_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 203 212 oligomers oligomeric_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 216 225 Fibrillar protein_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 226 235 oligomers oligomeric_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 281 293 nonfibrillar protein_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 294 303 oligomers oligomeric_state Two general types of endogenous Aβ oligomers have been observed: Aβ oligomers that occur on a pathway to fibrils, or “fibrillar oligomers”, and Aβ oligomers that evade a fibrillar fate, or “nonfibrillar oligomers”.− Fibrillar oligomers accumulate in Alzheimer’s disease later than nonfibrillar oligomers and coincide with the deposition of plaques. DISCUSS | |
| 0 12 Nonfibrillar protein_state Nonfibrillar oligomers accumulate early in Alzheimer’s disease before plaque deposition. DISCUSS | |
| 13 22 oligomers oligomeric_state Nonfibrillar oligomers accumulate early in Alzheimer’s disease before plaque deposition. DISCUSS | |
| 0 9 Fibrillar protein_state Fibrillar and nonfibrillar oligomers have structurally distinct characteristics, which are reflected in their reactivity with the fibril-specific OC antibody and the oligomer-specific A11 antibody. DISCUSS | |
| 14 26 nonfibrillar protein_state Fibrillar and nonfibrillar oligomers have structurally distinct characteristics, which are reflected in their reactivity with the fibril-specific OC antibody and the oligomer-specific A11 antibody. DISCUSS | |
| 27 36 oligomers oligomeric_state Fibrillar and nonfibrillar oligomers have structurally distinct characteristics, which are reflected in their reactivity with the fibril-specific OC antibody and the oligomer-specific A11 antibody. DISCUSS | |
| 166 174 oligomer oligomeric_state Fibrillar and nonfibrillar oligomers have structurally distinct characteristics, which are reflected in their reactivity with the fibril-specific OC antibody and the oligomer-specific A11 antibody. DISCUSS | |
| 0 9 Fibrillar protein_state Fibrillar oligomers are recognized by the OC antibody but not the A11 antibody, whereas nonfibrillar oligomers are recognized by the A11 antibody but not the OC antibody. DISCUSS | |
| 10 19 oligomers oligomeric_state Fibrillar oligomers are recognized by the OC antibody but not the A11 antibody, whereas nonfibrillar oligomers are recognized by the A11 antibody but not the OC antibody. DISCUSS | |
| 88 100 nonfibrillar protein_state Fibrillar oligomers are recognized by the OC antibody but not the A11 antibody, whereas nonfibrillar oligomers are recognized by the A11 antibody but not the OC antibody. DISCUSS | |
| 101 110 oligomers oligomeric_state Fibrillar oligomers are recognized by the OC antibody but not the A11 antibody, whereas nonfibrillar oligomers are recognized by the A11 antibody but not the OC antibody. DISCUSS | |
| 46 48 Aβ protein These criteria have been used to classify the Aβ oligomers that accumulate in vivo. DISCUSS | |
| 49 58 oligomers oligomeric_state These criteria have been used to classify the Aβ oligomers that accumulate in vivo. DISCUSS | |
| 0 2 Aβ protein Aβ dimers have been classified as fibrillar oligomers, whereas Aβ trimers, Aβ*56, and APFs have been classified as nonfibrillar oligomers. DISCUSS | |
| 3 9 dimers oligomeric_state Aβ dimers have been classified as fibrillar oligomers, whereas Aβ trimers, Aβ*56, and APFs have been classified as nonfibrillar oligomers. DISCUSS | |
| 34 43 fibrillar protein_state Aβ dimers have been classified as fibrillar oligomers, whereas Aβ trimers, Aβ*56, and APFs have been classified as nonfibrillar oligomers. DISCUSS | |
| 44 53 oligomers oligomeric_state Aβ dimers have been classified as fibrillar oligomers, whereas Aβ trimers, Aβ*56, and APFs have been classified as nonfibrillar oligomers. DISCUSS | |
| 63 65 Aβ protein Aβ dimers have been classified as fibrillar oligomers, whereas Aβ trimers, Aβ*56, and APFs have been classified as nonfibrillar oligomers. DISCUSS | |
| 66 73 trimers oligomeric_state Aβ dimers have been classified as fibrillar oligomers, whereas Aβ trimers, Aβ*56, and APFs have been classified as nonfibrillar oligomers. DISCUSS | |
| 75 80 Aβ*56 complex_assembly Aβ dimers have been classified as fibrillar oligomers, whereas Aβ trimers, Aβ*56, and APFs have been classified as nonfibrillar oligomers. DISCUSS | |
| 86 90 APFs complex_assembly Aβ dimers have been classified as fibrillar oligomers, whereas Aβ trimers, Aβ*56, and APFs have been classified as nonfibrillar oligomers. DISCUSS | |
| 115 127 nonfibrillar protein_state Aβ dimers have been classified as fibrillar oligomers, whereas Aβ trimers, Aβ*56, and APFs have been classified as nonfibrillar oligomers. DISCUSS | |
| 128 137 oligomers oligomeric_state Aβ dimers have been classified as fibrillar oligomers, whereas Aβ trimers, Aβ*56, and APFs have been classified as nonfibrillar oligomers. DISCUSS | |
| 67 79 nonfibrillar protein_state Larson and Lesné proposed a model for the endogenous production of nonfibrillar oligomers that explains these observations. DISCUSS | |
| 80 89 oligomers oligomeric_state Larson and Lesné proposed a model for the endogenous production of nonfibrillar oligomers that explains these observations. DISCUSS | |
| 15 21 folded protein_state In this model, folded Aβ monomer assembles into a trimer, the trimer further assembles into hexamers and dodecamers, and the dodecamers further assemble to form annular protofibrils. DISCUSS | |
| 22 24 Aβ protein In this model, folded Aβ monomer assembles into a trimer, the trimer further assembles into hexamers and dodecamers, and the dodecamers further assemble to form annular protofibrils. DISCUSS | |
| 25 32 monomer oligomeric_state In this model, folded Aβ monomer assembles into a trimer, the trimer further assembles into hexamers and dodecamers, and the dodecamers further assemble to form annular protofibrils. DISCUSS | |
| 50 56 trimer oligomeric_state In this model, folded Aβ monomer assembles into a trimer, the trimer further assembles into hexamers and dodecamers, and the dodecamers further assemble to form annular protofibrils. DISCUSS | |
| 62 68 trimer oligomeric_state In this model, folded Aβ monomer assembles into a trimer, the trimer further assembles into hexamers and dodecamers, and the dodecamers further assemble to form annular protofibrils. DISCUSS | |
| 92 100 hexamers oligomeric_state In this model, folded Aβ monomer assembles into a trimer, the trimer further assembles into hexamers and dodecamers, and the dodecamers further assemble to form annular protofibrils. DISCUSS | |
| 105 115 dodecamers oligomeric_state In this model, folded Aβ monomer assembles into a trimer, the trimer further assembles into hexamers and dodecamers, and the dodecamers further assemble to form annular protofibrils. DISCUSS | |
| 125 135 dodecamers oligomeric_state In this model, folded Aβ monomer assembles into a trimer, the trimer further assembles into hexamers and dodecamers, and the dodecamers further assemble to form annular protofibrils. DISCUSS | |
| 161 181 annular protofibrils complex_assembly In this model, folded Aβ monomer assembles into a trimer, the trimer further assembles into hexamers and dodecamers, and the dodecamers further assemble to form annular protofibrils. DISCUSS | |
| 29 38 peptide 2 mutant The hierarchical assembly of peptide 2 is consistent with this model; and the trimer, dodecamer, and annular pore formed by peptide 2 may share similarities to the trimers, Aβ*56, and APFs observed in vivo. DISCUSS | |
| 78 84 trimer oligomeric_state The hierarchical assembly of peptide 2 is consistent with this model; and the trimer, dodecamer, and annular pore formed by peptide 2 may share similarities to the trimers, Aβ*56, and APFs observed in vivo. DISCUSS | |
| 86 95 dodecamer oligomeric_state The hierarchical assembly of peptide 2 is consistent with this model; and the trimer, dodecamer, and annular pore formed by peptide 2 may share similarities to the trimers, Aβ*56, and APFs observed in vivo. DISCUSS | |
| 101 113 annular pore site The hierarchical assembly of peptide 2 is consistent with this model; and the trimer, dodecamer, and annular pore formed by peptide 2 may share similarities to the trimers, Aβ*56, and APFs observed in vivo. DISCUSS | |
| 124 133 peptide 2 mutant The hierarchical assembly of peptide 2 is consistent with this model; and the trimer, dodecamer, and annular pore formed by peptide 2 may share similarities to the trimers, Aβ*56, and APFs observed in vivo. DISCUSS | |
| 164 171 trimers oligomeric_state The hierarchical assembly of peptide 2 is consistent with this model; and the trimer, dodecamer, and annular pore formed by peptide 2 may share similarities to the trimers, Aβ*56, and APFs observed in vivo. DISCUSS | |
| 173 178 Aβ*56 complex_assembly The hierarchical assembly of peptide 2 is consistent with this model; and the trimer, dodecamer, and annular pore formed by peptide 2 may share similarities to the trimers, Aβ*56, and APFs observed in vivo. DISCUSS | |
| 184 188 APFs complex_assembly The hierarchical assembly of peptide 2 is consistent with this model; and the trimer, dodecamer, and annular pore formed by peptide 2 may share similarities to the trimers, Aβ*56, and APFs observed in vivo. DISCUSS | |
| 49 55 trimer oligomeric_state At this point, we can only speculate whether the trimer and dodecamer formed by peptide 2 share structural similarities to Aβ trimers and Aβ*56, as little is known about the structure of Aβ trimers and Aβ*56. DISCUSS | |
| 60 69 dodecamer oligomeric_state At this point, we can only speculate whether the trimer and dodecamer formed by peptide 2 share structural similarities to Aβ trimers and Aβ*56, as little is known about the structure of Aβ trimers and Aβ*56. DISCUSS | |
| 80 89 peptide 2 mutant At this point, we can only speculate whether the trimer and dodecamer formed by peptide 2 share structural similarities to Aβ trimers and Aβ*56, as little is known about the structure of Aβ trimers and Aβ*56. DISCUSS | |
| 123 125 Aβ protein At this point, we can only speculate whether the trimer and dodecamer formed by peptide 2 share structural similarities to Aβ trimers and Aβ*56, as little is known about the structure of Aβ trimers and Aβ*56. DISCUSS | |
| 126 133 trimers oligomeric_state At this point, we can only speculate whether the trimer and dodecamer formed by peptide 2 share structural similarities to Aβ trimers and Aβ*56, as little is known about the structure of Aβ trimers and Aβ*56. DISCUSS | |
| 138 143 Aβ*56 complex_assembly At this point, we can only speculate whether the trimer and dodecamer formed by peptide 2 share structural similarities to Aβ trimers and Aβ*56, as little is known about the structure of Aβ trimers and Aβ*56. DISCUSS | |
| 174 183 structure evidence At this point, we can only speculate whether the trimer and dodecamer formed by peptide 2 share structural similarities to Aβ trimers and Aβ*56, as little is known about the structure of Aβ trimers and Aβ*56. DISCUSS | |
| 187 189 Aβ protein At this point, we can only speculate whether the trimer and dodecamer formed by peptide 2 share structural similarities to Aβ trimers and Aβ*56, as little is known about the structure of Aβ trimers and Aβ*56. DISCUSS | |
| 190 197 trimers oligomeric_state At this point, we can only speculate whether the trimer and dodecamer formed by peptide 2 share structural similarities to Aβ trimers and Aβ*56, as little is known about the structure of Aβ trimers and Aβ*56. DISCUSS | |
| 202 207 Aβ*56 complex_assembly At this point, we can only speculate whether the trimer and dodecamer formed by peptide 2 share structural similarities to Aβ trimers and Aβ*56, as little is known about the structure of Aβ trimers and Aβ*56. DISCUSS | |
| 4 33 crystallographically observed evidence The crystallographically observed annular pore formed by peptide 2 is morphologically similar to the APFs formed by full-length Aβ. DISCUSS | |
| 34 46 annular pore site The crystallographically observed annular pore formed by peptide 2 is morphologically similar to the APFs formed by full-length Aβ. DISCUSS | |
| 57 66 peptide 2 mutant The crystallographically observed annular pore formed by peptide 2 is morphologically similar to the APFs formed by full-length Aβ. DISCUSS | |
| 101 105 APFs complex_assembly The crystallographically observed annular pore formed by peptide 2 is morphologically similar to the APFs formed by full-length Aβ. DISCUSS | |
| 116 127 full-length protein_state The crystallographically observed annular pore formed by peptide 2 is morphologically similar to the APFs formed by full-length Aβ. DISCUSS | |
| 128 130 Aβ protein The crystallographically observed annular pore formed by peptide 2 is morphologically similar to the APFs formed by full-length Aβ. DISCUSS | |
| 4 16 annular pore site The annular pore formed by peptide 2 is comparable in size to the APFs prepared in vitro or isolated from Alzheimer’s brains (Figure 7 and Table 1). DISCUSS | |
| 27 36 peptide 2 mutant The annular pore formed by peptide 2 is comparable in size to the APFs prepared in vitro or isolated from Alzheimer’s brains (Figure 7 and Table 1). DISCUSS | |
| 66 70 APFs complex_assembly The annular pore formed by peptide 2 is comparable in size to the APFs prepared in vitro or isolated from Alzheimer’s brains (Figure 7 and Table 1). DISCUSS | |
| 21 25 APFs complex_assembly The varying sizes of APFs formed by full-length Aβ might result from differences in the number of oligomer subunits comprising each APF. DISCUSS | |
| 36 47 full-length protein_state The varying sizes of APFs formed by full-length Aβ might result from differences in the number of oligomer subunits comprising each APF. DISCUSS | |
| 48 50 Aβ protein The varying sizes of APFs formed by full-length Aβ might result from differences in the number of oligomer subunits comprising each APF. DISCUSS | |
| 98 106 oligomer oligomeric_state The varying sizes of APFs formed by full-length Aβ might result from differences in the number of oligomer subunits comprising each APF. DISCUSS | |
| 107 115 subunits structure_element The varying sizes of APFs formed by full-length Aβ might result from differences in the number of oligomer subunits comprising each APF. DISCUSS | |
| 132 135 APF complex_assembly The varying sizes of APFs formed by full-length Aβ might result from differences in the number of oligomer subunits comprising each APF. DISCUSS | |
| 13 25 annular pore site Although the annular pore formed by peptide 2 contains five dodecamer subunits, pores containing fewer or more subunits can easily be envisioned. DISCUSS | |
| 36 45 peptide 2 mutant Although the annular pore formed by peptide 2 contains five dodecamer subunits, pores containing fewer or more subunits can easily be envisioned. DISCUSS | |
| 60 69 dodecamer oligomeric_state Although the annular pore formed by peptide 2 contains five dodecamer subunits, pores containing fewer or more subunits can easily be envisioned. DISCUSS | |
| 70 78 subunits structure_element Although the annular pore formed by peptide 2 contains five dodecamer subunits, pores containing fewer or more subunits can easily be envisioned. DISCUSS | |
| 80 85 pores site Although the annular pore formed by peptide 2 contains five dodecamer subunits, pores containing fewer or more subunits can easily be envisioned. DISCUSS | |
| 111 119 subunits structure_element Although the annular pore formed by peptide 2 contains five dodecamer subunits, pores containing fewer or more subunits can easily be envisioned. DISCUSS | |
| 4 14 dodecamers oligomeric_state The dodecamers that comprise the annular pore exhibit two modes of assembly—eclipsed interactions and staggered interactions between the F20 faces of trimers within dodecamers. DISCUSS | |
| 33 45 annular pore site The dodecamers that comprise the annular pore exhibit two modes of assembly—eclipsed interactions and staggered interactions between the F20 faces of trimers within dodecamers. DISCUSS | |
| 76 84 eclipsed protein_state The dodecamers that comprise the annular pore exhibit two modes of assembly—eclipsed interactions and staggered interactions between the F20 faces of trimers within dodecamers. DISCUSS | |
| 102 111 staggered protein_state The dodecamers that comprise the annular pore exhibit two modes of assembly—eclipsed interactions and staggered interactions between the F20 faces of trimers within dodecamers. DISCUSS | |
| 137 140 F20 residue_name_number The dodecamers that comprise the annular pore exhibit two modes of assembly—eclipsed interactions and staggered interactions between the F20 faces of trimers within dodecamers. DISCUSS | |
| 150 157 trimers oligomeric_state The dodecamers that comprise the annular pore exhibit two modes of assembly—eclipsed interactions and staggered interactions between the F20 faces of trimers within dodecamers. DISCUSS | |
| 165 175 dodecamers oligomeric_state The dodecamers that comprise the annular pore exhibit two modes of assembly—eclipsed interactions and staggered interactions between the F20 faces of trimers within dodecamers. DISCUSS | |
| 72 82 dodecamers oligomeric_state These two modes of assembly might reflect a dynamic interaction between dodecamers, which could permit assemblies of more dodecamers into larger annular pores. DISCUSS | |
| 122 132 dodecamers oligomeric_state These two modes of assembly might reflect a dynamic interaction between dodecamers, which could permit assemblies of more dodecamers into larger annular pores. DISCUSS | |
| 145 158 annular pores site These two modes of assembly might reflect a dynamic interaction between dodecamers, which could permit assemblies of more dodecamers into larger annular pores. DISCUSS | |
| 21 33 annular pore site Surface views of the annular pore formed by peptide 2. (A) Top view. FIG | |
| 44 53 peptide 2 mutant Surface views of the annular pore formed by peptide 2. (A) Top view. FIG | |
| 0 13 Annular Pores site Annular Pores Formed by Aβ and Peptide 2 TABLE | |
| 24 26 Aβ protein Annular Pores Formed by Aβ and Peptide 2 TABLE | |
| 31 40 Peptide 2 mutant Annular Pores Formed by Aβ and Peptide 2 TABLE | |
| 0 12 annular pore site "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 75 82 peptide chemical "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 102 123 X-ray crystallography experimental_method "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 126 135 synthetic protein_state "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 136 138 Aβ protein "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 156 159 TEM experimental_method "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 172 174 Aβ protein "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 194 197 AFM experimental_method "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 210 212 Aβ protein "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 234 237 TEM experimental_method "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 276 279 TEM experimental_method "annular pore source outer diameter inner diameter observation method peptide 2 ∼11–12 nm ∼2 nm X-ray crystallography synthetic Aβ 7–10 nm 1.5–2 nm TEM synthetic Aβ 16 nm not reported AFM synthetic Aβ 8–25 nm not reported TEM Alzheimer’s brain 11–14 nm 2.5–4 nm TEM " TABLE | |
| 0 8 Dot blot experimental_method Dot blot analysis shows that peptide 2 is reactive toward the A11 antibody (Figure S5). DISCUSS | |
| 29 38 peptide 2 mutant Dot blot analysis shows that peptide 2 is reactive toward the A11 antibody (Figure S5). DISCUSS | |
| 30 39 peptide 2 mutant This reactivity suggests that peptide 2 forms oligomers in solution that share structural similarities to the nonfibrillar oligomers formed by full-length Aβ. DISCUSS | |
| 46 55 oligomers oligomeric_state This reactivity suggests that peptide 2 forms oligomers in solution that share structural similarities to the nonfibrillar oligomers formed by full-length Aβ. DISCUSS | |
| 110 122 nonfibrillar protein_state This reactivity suggests that peptide 2 forms oligomers in solution that share structural similarities to the nonfibrillar oligomers formed by full-length Aβ. DISCUSS | |
| 123 132 oligomers oligomeric_state This reactivity suggests that peptide 2 forms oligomers in solution that share structural similarities to the nonfibrillar oligomers formed by full-length Aβ. DISCUSS | |
| 143 154 full-length protein_state This reactivity suggests that peptide 2 forms oligomers in solution that share structural similarities to the nonfibrillar oligomers formed by full-length Aβ. DISCUSS | |
| 155 157 Aβ protein This reactivity suggests that peptide 2 forms oligomers in solution that share structural similarities to the nonfibrillar oligomers formed by full-length Aβ. DISCUSS | |
| 57 66 peptide 2 mutant Further studies are needed to elucidate the species that peptide 2 forms in solution and to study their biological properties. DISCUSS | |
| 47 50 SEC experimental_method Preliminary attempts to study these species by SEC and SDS-PAGE have not provided a clear measure of the structures formed in solution. DISCUSS | |
| 55 63 SDS-PAGE experimental_method Preliminary attempts to study these species by SEC and SDS-PAGE have not provided a clear measure of the structures formed in solution. DISCUSS | |
| 105 115 structures evidence Preliminary attempts to study these species by SEC and SDS-PAGE have not provided a clear measure of the structures formed in solution. DISCUSS | |
| 31 40 oligomers oligomeric_state The difficulty in studying the oligomers formed in solution may reflect the propensity of the dodecamer to assemble on all four F20 faces. DISCUSS | |
| 94 103 dodecamer oligomeric_state The difficulty in studying the oligomers formed in solution may reflect the propensity of the dodecamer to assemble on all four F20 faces. DISCUSS | |
| 128 131 F20 residue_name_number The difficulty in studying the oligomers formed in solution may reflect the propensity of the dodecamer to assemble on all four F20 faces. DISCUSS | |
| 4 36 X-ray crystallographic structure evidence The X-ray crystallographic structure and A11 reactivity of peptide 2 support the model proposed by Larsen and Lesné and suggest that β-hairpins constitute a fundamental building block for nonfibrillar oligomers. DISCUSS | |
| 59 68 peptide 2 mutant The X-ray crystallographic structure and A11 reactivity of peptide 2 support the model proposed by Larsen and Lesné and suggest that β-hairpins constitute a fundamental building block for nonfibrillar oligomers. DISCUSS | |
| 133 143 β-hairpins structure_element The X-ray crystallographic structure and A11 reactivity of peptide 2 support the model proposed by Larsen and Lesné and suggest that β-hairpins constitute a fundamental building block for nonfibrillar oligomers. DISCUSS | |
| 188 200 nonfibrillar protein_state The X-ray crystallographic structure and A11 reactivity of peptide 2 support the model proposed by Larsen and Lesné and suggest that β-hairpins constitute a fundamental building block for nonfibrillar oligomers. DISCUSS | |
| 201 210 oligomers oligomeric_state The X-ray crystallographic structure and A11 reactivity of peptide 2 support the model proposed by Larsen and Lesné and suggest that β-hairpins constitute a fundamental building block for nonfibrillar oligomers. DISCUSS | |
| 11 21 β-hairpins structure_element What makes β-hairpins special is that three β-hairpins can nestle together to form trimers, stabilized by a network of hydrogen bonds and hydrophobic interactions. DISCUSS | |
| 44 54 β-hairpins structure_element What makes β-hairpins special is that three β-hairpins can nestle together to form trimers, stabilized by a network of hydrogen bonds and hydrophobic interactions. DISCUSS | |
| 83 90 trimers oligomeric_state What makes β-hairpins special is that three β-hairpins can nestle together to form trimers, stabilized by a network of hydrogen bonds and hydrophobic interactions. DISCUSS | |
| 119 133 hydrogen bonds bond_interaction What makes β-hairpins special is that three β-hairpins can nestle together to form trimers, stabilized by a network of hydrogen bonds and hydrophobic interactions. DISCUSS | |
| 138 162 hydrophobic interactions bond_interaction What makes β-hairpins special is that three β-hairpins can nestle together to form trimers, stabilized by a network of hydrogen bonds and hydrophobic interactions. DISCUSS | |
| 39 41 Aβ protein This mode of assembly is not unique to Aβ. DISCUSS | |
| 4 17 foldon domain structure_element The foldon domain of bacteriophage T4 fibritin is composed of three β-hairpins that assemble into a triangular trimer similar to the triangular trimer formed by peptide 2. DISCUSS | |
| 21 37 bacteriophage T4 species The foldon domain of bacteriophage T4 fibritin is composed of three β-hairpins that assemble into a triangular trimer similar to the triangular trimer formed by peptide 2. DISCUSS | |
| 38 46 fibritin protein The foldon domain of bacteriophage T4 fibritin is composed of three β-hairpins that assemble into a triangular trimer similar to the triangular trimer formed by peptide 2. DISCUSS | |
| 68 78 β-hairpins structure_element The foldon domain of bacteriophage T4 fibritin is composed of three β-hairpins that assemble into a triangular trimer similar to the triangular trimer formed by peptide 2. DISCUSS | |
| 100 110 triangular protein_state The foldon domain of bacteriophage T4 fibritin is composed of three β-hairpins that assemble into a triangular trimer similar to the triangular trimer formed by peptide 2. DISCUSS | |
| 111 117 trimer oligomeric_state The foldon domain of bacteriophage T4 fibritin is composed of three β-hairpins that assemble into a triangular trimer similar to the triangular trimer formed by peptide 2. DISCUSS | |
| 133 143 triangular protein_state The foldon domain of bacteriophage T4 fibritin is composed of three β-hairpins that assemble into a triangular trimer similar to the triangular trimer formed by peptide 2. DISCUSS | |
| 144 150 trimer oligomeric_state The foldon domain of bacteriophage T4 fibritin is composed of three β-hairpins that assemble into a triangular trimer similar to the triangular trimer formed by peptide 2. DISCUSS | |
| 161 170 peptide 2 mutant The foldon domain of bacteriophage T4 fibritin is composed of three β-hairpins that assemble into a triangular trimer similar to the triangular trimer formed by peptide 2. DISCUSS | |
| 70 79 β-hairpin structure_element Additionally, our research group has observed a similar assembly of a β-hairpin peptide derived from β2-microglobulin. DISCUSS | |
| 101 117 β2-microglobulin protein Additionally, our research group has observed a similar assembly of a β-hairpin peptide derived from β2-microglobulin. DISCUSS | |
| 77 84 trimers oligomeric_state Although we began these studies with a relatively simple hypothesis—that the trimers and dodecamers formed by peptide 1 could accommodate the Aβ24–29 loop—an even more exciting finding has emerged—that the dodecamers can assemble to form annular pores. CONCL | |
| 89 99 dodecamers oligomeric_state Although we began these studies with a relatively simple hypothesis—that the trimers and dodecamers formed by peptide 1 could accommodate the Aβ24–29 loop—an even more exciting finding has emerged—that the dodecamers can assemble to form annular pores. CONCL | |
| 110 119 peptide 1 mutant Although we began these studies with a relatively simple hypothesis—that the trimers and dodecamers formed by peptide 1 could accommodate the Aβ24–29 loop—an even more exciting finding has emerged—that the dodecamers can assemble to form annular pores. CONCL | |
| 142 144 Aβ protein Although we began these studies with a relatively simple hypothesis—that the trimers and dodecamers formed by peptide 1 could accommodate the Aβ24–29 loop—an even more exciting finding has emerged—that the dodecamers can assemble to form annular pores. CONCL | |
| 144 149 24–29 residue_range Although we began these studies with a relatively simple hypothesis—that the trimers and dodecamers formed by peptide 1 could accommodate the Aβ24–29 loop—an even more exciting finding has emerged—that the dodecamers can assemble to form annular pores. CONCL | |
| 150 154 loop structure_element Although we began these studies with a relatively simple hypothesis—that the trimers and dodecamers formed by peptide 1 could accommodate the Aβ24–29 loop—an even more exciting finding has emerged—that the dodecamers can assemble to form annular pores. CONCL | |
| 206 216 dodecamers oligomeric_state Although we began these studies with a relatively simple hypothesis—that the trimers and dodecamers formed by peptide 1 could accommodate the Aβ24–29 loop—an even more exciting finding has emerged—that the dodecamers can assemble to form annular pores. CONCL | |
| 238 251 annular pores site Although we began these studies with a relatively simple hypothesis—that the trimers and dodecamers formed by peptide 1 could accommodate the Aβ24–29 loop—an even more exciting finding has emerged—that the dodecamers can assemble to form annular pores. CONCL | |
| 54 86 X-ray crystallographic structure evidence This finding could not have been anticipated from the X-ray crystallographic structure of peptide 1 and reveals a new level of hierarchical assembly that recapitulates micrographic observations of annular protofibrils. CONCL | |
| 90 99 peptide 1 mutant This finding could not have been anticipated from the X-ray crystallographic structure of peptide 1 and reveals a new level of hierarchical assembly that recapitulates micrographic observations of annular protofibrils. CONCL | |
| 197 217 annular protofibrils complex_assembly This finding could not have been anticipated from the X-ray crystallographic structure of peptide 1 and reveals a new level of hierarchical assembly that recapitulates micrographic observations of annular protofibrils. CONCL | |
| 4 33 crystallographically observed evidence The crystallographically observed dodecamer, in turn, recapitulates the observation of Aβ*56, which appears to be a dodecamer of Aβ. CONCL | |
| 34 43 dodecamer oligomeric_state The crystallographically observed dodecamer, in turn, recapitulates the observation of Aβ*56, which appears to be a dodecamer of Aβ. CONCL | |
| 87 92 Aβ*56 complex_assembly The crystallographically observed dodecamer, in turn, recapitulates the observation of Aβ*56, which appears to be a dodecamer of Aβ. CONCL | |
| 116 125 dodecamer oligomeric_state The crystallographically observed dodecamer, in turn, recapitulates the observation of Aβ*56, which appears to be a dodecamer of Aβ. CONCL | |
| 129 131 Aβ protein The crystallographically observed dodecamer, in turn, recapitulates the observation of Aβ*56, which appears to be a dodecamer of Aβ. CONCL | |
| 4 33 crystallographically observed evidence The crystallographically observed trimer recapitulates the Aβ trimers that are observed even before the onset of symptoms in Alzheimer’s disease. CONCL | |
| 34 40 trimer oligomeric_state The crystallographically observed trimer recapitulates the Aβ trimers that are observed even before the onset of symptoms in Alzheimer’s disease. CONCL | |
| 59 61 Aβ protein The crystallographically observed trimer recapitulates the Aβ trimers that are observed even before the onset of symptoms in Alzheimer’s disease. CONCL | |
| 62 69 trimers oligomeric_state The crystallographically observed trimer recapitulates the Aβ trimers that are observed even before the onset of symptoms in Alzheimer’s disease. CONCL | |
| 29 31 Aβ protein Our approach of constraining Aβ17–36 into a β-hairpin conformation and blocking aggregation with an N-methyl group has allowed us to crystallize a large fragment of what is generally considered to be an uncrystallizable peptide. CONCL | |
| 31 36 17–36 residue_range Our approach of constraining Aβ17–36 into a β-hairpin conformation and blocking aggregation with an N-methyl group has allowed us to crystallize a large fragment of what is generally considered to be an uncrystallizable peptide. CONCL | |
| 44 53 β-hairpin structure_element Our approach of constraining Aβ17–36 into a β-hairpin conformation and blocking aggregation with an N-methyl group has allowed us to crystallize a large fragment of what is generally considered to be an uncrystallizable peptide. CONCL | |
| 133 144 crystallize experimental_method Our approach of constraining Aβ17–36 into a β-hairpin conformation and blocking aggregation with an N-methyl group has allowed us to crystallize a large fragment of what is generally considered to be an uncrystallizable peptide. CONCL | |
| 100 111 crystallize experimental_method We believe this iterative, “bottom up” approach of identifying the minimal modification required to crystallize Aβ peptides will ultimately allow larger fragments of Aβ to be crystallized, thus providing greater insights into the structures of Aβ oligomers. CONCL | |
| 112 114 Aβ protein We believe this iterative, “bottom up” approach of identifying the minimal modification required to crystallize Aβ peptides will ultimately allow larger fragments of Aβ to be crystallized, thus providing greater insights into the structures of Aβ oligomers. CONCL | |
| 166 168 Aβ protein We believe this iterative, “bottom up” approach of identifying the minimal modification required to crystallize Aβ peptides will ultimately allow larger fragments of Aβ to be crystallized, thus providing greater insights into the structures of Aβ oligomers. CONCL | |
| 175 187 crystallized experimental_method We believe this iterative, “bottom up” approach of identifying the minimal modification required to crystallize Aβ peptides will ultimately allow larger fragments of Aβ to be crystallized, thus providing greater insights into the structures of Aβ oligomers. CONCL | |
| 230 240 structures evidence We believe this iterative, “bottom up” approach of identifying the minimal modification required to crystallize Aβ peptides will ultimately allow larger fragments of Aβ to be crystallized, thus providing greater insights into the structures of Aβ oligomers. CONCL | |
| 244 246 Aβ protein We believe this iterative, “bottom up” approach of identifying the minimal modification required to crystallize Aβ peptides will ultimately allow larger fragments of Aβ to be crystallized, thus providing greater insights into the structures of Aβ oligomers. CONCL | |
| 247 256 oligomers oligomeric_state We believe this iterative, “bottom up” approach of identifying the minimal modification required to crystallize Aβ peptides will ultimately allow larger fragments of Aβ to be crystallized, thus providing greater insights into the structures of Aβ oligomers. CONCL | |