LiteFold/DisProt huggingface dataset:
Protein: DP00065 (UniProt O86488)
Region: residues 569	to 1123
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Because, except for a blue shift of the minimum to 197 nm, the spectrum of metal-free B1–B5 at 25 °C is very similar, this form must contain very little organized secondary structure.
Protein: DP00065 (UniProt O86488)
Region: residues 569	to 1123
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In contrast, the Ca2+-loaded protein shows discrete peaks: one positive peak at 228 nm, which may be attributable to aromatic residues (26), and two negative peaks at 215 and 195 nm.
Protein: DP00065 (UniProt O86488)
Region: residues 569	to 1123
Annotation: calcium ion binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In contrast, the Ca2+-loaded protein shows discrete peaks: one positive peak at 228 nm, which may be attributable to aromatic residues (26), and two negative peaks at 215 and 195 nm.
Protein: DP00065 (UniProt O86488)
Region: residues 569	to 1123
Annotation: disorder (Structural state)
Evidence: near-UV circular dichroism evidence used in manual assertion
Supporting statements:
Removal of Ca2+ changed the intensity of ellipticity only slightly, with a 2-nm blue shift, indicating that microenvironment of the Tyr residues in apoB1–B5 is asymmetric and therefore structured.
Protein: DP00065 (UniProt O86488)
Region: residues 569	to 1123
Annotation: disorder to order (Structural transition)
Evidence: near-UV circular dichroism evidence used in manual assertion
Supporting statements:
Removal of Ca2+ changed the intensity of ellipticity only slightly, with a 2-nm blue shift, indicating that microenvironment of the Tyr residues in apoB1–B5 is asymmetric and therefore structured.
Protein: DP00065 (UniProt O86488)
Region: residues 569	to 1123
Annotation: calcium ion binding (Molecular function)
Evidence: near-UV circular dichroism evidence used in manual assertion
Supporting statements:
Removal of Ca2+ changed the intensity of ellipticity only slightly, with a 2-nm blue shift, indicating that microenvironment of the Tyr residues in apoB1–B5 is asymmetric and therefore structured.
Protein: DP00065 (UniProt O86488)
Region: residues 569	to 1123
Annotation: disorder (Structural state)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
The spectrum of the metal-free protein is quite similar to that of the guanidine-HCl-denatured form, although its intensity is 20% higher, and the maximum blue shifted by 5 nm.
Protein: DP00065 (UniProt O86488)
Region: residues 569	to 1123
Annotation: disorder to order (Structural transition)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
The Ca2+-saturated protein shows a 2.5-fold higher fluorescence intensity and a blue shift from 345 to 323 nm compared with the metal-free state, suggesting that with Ca2+ binding a well organized hydrophobic core is formed around the Trp residue (31).
Protein: DP00065 (UniProt O86488)
Region: residues 569	to 1123
Annotation: calcium ion binding (Molecular function)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
The Ca2+-saturated protein shows a 2.5-fold higher fluorescence intensity and a blue shift from 345 to 323 nm compared with the metal-free state, suggesting that with Ca2+ binding a well organized hydrophobic core is formed around the Trp residue (31).
Protein: DP00065 (UniProt O86488)
Region: residues 1117	to 1250
Annotation: disorder (Structural state)
Evidence: curator inference from database used in manual assertion
Supporting statements:
This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)
Protein: DP00067 (UniProt Q57733)
Region: residues 1	to 32
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The amino-terminal 32 residues are highly disordered, but from residue 33 onwards, including the entire α-crystallin domain (residues 46–135) and thecarboxy-terminal extension, they are well ordered.
Cross-references: PDB:1SHS
Protein: DP00067 (UniProt Q57733)
Region: residues 1	to 32
Annotation: flexible N-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The amino-terminal 32 residues are highly disordered, but from residue 33 onwards, including the entire α-crystallin domain (residues 46–135) and thecarboxy-terminal extension, they are well ordered.
Protein: DP00067 (UniProt Q57733)
Region: residues 1	to 33
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The region is missing from the pdb structure.
Cross-references: PDB:4I88
Protein: DP00067 (UniProt Q57733)
Region: residues 1	to 33
Annotation: flexible N-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The region is missing from the pdb structure.
Cross-references: PDB:4I88
Protein: DP00068 (UniProt P60881)
Region: residues 120	to 206
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Synaptobrevin and both SNAP-25 fragments were largely unstructured, similar to previous results (not shown; see refs 18 and 19).
Protein: DP00068 (UniProt P60881)
Region: residues 2	to 83
Annotation: protein binding (Molecular function)
Evidence: native protein gel electrophoresis evidence used in manual assertion
Supporting statements:
Furthermore, the syntaxin fragment formed stable complexes either with the N-terminal or with both fragments of SNAP-25 but not with the C-terminal fragment alone (Figure 4, lanes 9 and 10), again consistent with previous results (18).
Protein: DP00068 (UniProt P60881)
Region: residues 2	to 83
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Formation of these subcomplexes was associated with an increase in α-helical content that was more pronounced than that observed previously for the full-length proteins (Figure 3, columns 13−15; see ref 18].
Protein: DP00068 (UniProt P60881)
Region: residues 2	to 83
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Formation of these subcomplexes was associated with an increase in α-helical content that was more pronounced than that observed previously for the full-length proteins (Figure 3, columns 13−15; see ref 18].
Protein: DP00068 (UniProt P60881)
Region: residues 84	to 119
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Analysis of the fragments derived from SNAP-25 revealed that both proteases excised the middle region which contains the putative membrane anchor domain. The resulting N- and C-terminal fragments remained in the SDS-resistant core complex. The N-terminal fragments generated by the two proteases were identical (residues 2−83). The C-terminal fragments generated by trypsin extended from residues 120 or 125 to the C-terminal end of the SNAP-25 construct, including the entire His6 tag.
Protein: DP00068 (UniProt P60881)
Region: residues 2	to 83
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Synaptobrevin and both SNAP-25 fragments were largely unstructured, similar to previous results (not shown; see refs 18 and 19).
Protein: DP00069 (UniProt P63027)
Region: residues 40	to 67
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In aqueous media, all peptides (alone or in mixtures) were unstructured, and neither increasing peptide concentration nor changing pH, ionic strength, or divalent cation concentration increased the α-helical content.
Protein: DP00069 (UniProt P63027)
Region: residues 40	to 67
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In the presence of increasing concentrations of TFE (Fig.2, A–C), there was a significant increase in the α-helical content. The minimal concentration at which the peptides underwent a transition from mostly unstructured to partially structured was approximately 30%.
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
NACP Exhibits Properties Characteristic of an Extended Protein. The exact molecular weight of the NACP used in this work was found to be [M + H+] = 14 463 (±4.6) by MALDI-TOF mass spectrometry, consistent with the molecular weight of 14 460 predicted on the basis of the encoded amino acid sequence. On SDS−polyacrylamide gel electrophoresis (SDS−PAGE), the protein exhibits an apparent Mr of approximately 19 000 (Uéda et al., 1993), which may be attributable to abnormally low binding of SDS by the highly acidic NACP C-terminal sequence. A similar abnormal mobility has been demonstrated by other highly charged proteins (Williams et al., 1986; Yoo & Albanesi, 1990; Thomas et al., 1991; Gast et al., 1995).
Protein: DP00070 (UniProt P37840)
Region: residues 100	to 140
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, the final 40 residues of αS exhibit secondary shifts that are more evenly distributed between the α and β regions of conformational space, suggesting that they are more highly unfolded and extended.
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer.
Our findings demonstrate that both human and rodent α-syn expressed in the central nervous system exist predominantly as an unfolded monomer.
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: lipid binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Far-UV CD spectroscopy performed at a protein concentration of 5 μM revealed that both native and heat-treated recombinant α-syn were mostly devoid of any significant secondary structure, as shown by a single spectral minimum at ~195 nm (Fig. 1C). Moreover, we confirmed that both native and denatured preparations are able to bind lipids and adopt an α-helical structure upon binding to 100-nm POPG small unilamellar vesicles.
Protein: DP00070 (UniProt P37840)
Region: residues 42	to 92
Annotation: disorder (Structural state)
Evidence: site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion
Supporting statements:
To advance the understanding of protein-micelle interactions, the present study concludes by showing that, in marked contrast to secondary structure stability, helix dynamics of SLAS-bound αS correlate with the degree of protein-induced departures from free micelle dimensions.
Cross-references: PDB:2KKW
Protein: DP00070 (UniProt P37840)
Region: residues 42	to 92
Annotation: disorder to order (Structural transition)
Evidence: site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion
Supporting statements:
To advance the understanding of protein-micelle interactions, the present study concludes by showing that, in marked contrast to secondary structure stability, helix dynamics of SLAS-bound αS correlate with the degree of protein-induced departures from free micelle dimensions.
Protein: DP00070 (UniProt P37840)
Region: residues 42	to 92
Annotation: lipid binding (Molecular function)
Evidence: site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion
Supporting statements:
To advance the understanding of protein-micelle interactions, the present study concludes by showing that, in marked contrast to secondary structure stability, helix dynamics of SLAS-bound αS correlate with the degree of protein-induced departures from free micelle dimensions.
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
α-Synuclein is a presynaptic protein associated to Parkinson's disease, which is unstructured when free in the cytoplasm and adopts α helical conformation when bound to vesicles.
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
α-Synuclein is a presynaptic protein associated to Parkinson's disease, which is unstructured when free in the cytoplasm and adopts α helical conformation when bound to vesicles.
Syn binds to MTs and folds upon interaction with the tubulin α2β2 tetramer
Our data confirmed that Syn is unfolded in the absence of the ligand, whereas an equimolar Syn/tubulin mixture gives an overall secondary structure CD signal, which is more intense than the sum of the signals of the two individual proteins (Fig. 2a). Moreover, the CD signal originating in the mixture shows a gain of signal at 220 nm, which is typical of α-helix structures. Considering that (i) the interaction of tubulin with ligands is widely studied and an increase in its α-helix content has never been observed, and (ii) Syn is a soluble, intrinsically unfolded protein which is able to adopt α-helix structure in adequate conditions
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: tubulin binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Syn binds to MTs and folds upon interaction with the tubulin α2β2 tetramer
Our data confirmed that Syn is unfolded in the absence of the ligand, whereas an equimolar Syn/tubulin mixture gives an overall secondary structure CD signal, which is more intense than the sum of the signals of the two individual proteins (Fig. 2a). Moreover, the CD signal originating in the mixture shows a gain of signal at 220 nm, which is typical of α-helix structures. Considering that (i) the interaction of tubulin with ligands is widely studied and an increase in its α-helix content has never been observed, and (ii) Syn is a soluble, intrinsically unfolded protein which is able to adopt α-helix structure in adequate conditions
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Far-UV CD data from wild-type αS in the presence and absence of SDS micelles, under conditions and protein concentrations (100 μM) identical to those used in the NMR experiments. A large conformational change is evident, with a high degree of helicity (indicated by the characteristic double minima at 208 and 222 nm) formed in the presence of micelles.
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 102
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
A comparison of this spectrum with an equivalent spectrum from the free protein (Figure 7), shows that the Cα chemical shifts of the micelle associated residues are in general larger by approximately 2 ppm than they are in the free protein. This provides strong evidence for significant, persistent helical structure in the micelle associated region of αS.
Thus, it appears that the interaction of αS with synthetic lipid vesicles is quite similar to its interaction with SDS detergent micelles, as nearly identical regions of the protein remain free from or are bound to the micelle or vesicle in both cases.
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 102
Annotation: lipid binding (Molecular function)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Our observations indicate a partition of αS into two functionally distinct regions. The N-terminal region is responsible for lipid binding. The NMR data suggest that the boundary for this region occurs between residues 102 and 103. Interestingly, the first three exons in the coding region of the αS gene encode residues 1 to 102, and a recent report indicates that the lipid binding capacity of αS is distributed across this region of the protein (Perrin et al., 2000). The close correspondence between the exon-defined boundary and the boundary we observe in our NMR data supports a distinct functional role (lipid binding) for this region of αS.
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
the disordered nature of monomeric α-synuclein is stably preserved in non-neuronal and neuronal cells
Our results show that exogenously delivered αSyn exists as an N-terminally acetylated, disordered and highly dynamic monomer in neuronal and non-neuronal cells, without detectable signs of oligomerization, spontaneous aggregation, or targeted degradation.
αSyn is disordered in mammalian cells
αSyn is N-terminally acetylated in cells
αSyn interacts with the cytoplasm
αSyn adopts compact structures in cells
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: disorder (Structural state)
Evidence: circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism (CD) and Fourier-transform infrared spectroscopy (FTIR) indicate the absence of significant amounts of secondary structure in NACP, while CD and ultraviolet spectroscopy suggest the lack of a hydrophobic core.
CD, UV, and FTIR Spectroscopy Indicate NACP Has a “Random Coil” Conformation.
These features indicate that NACP exists as a mixture of rapidly equilibrating extended conformers and is representative of a class of "natively unfolded" proteins, many of which potentiate protein-protein interactions.
NACP Is a “Natively Unfolded” Protein. The results presented herein provide evidence that, in solution, NACP exists as a mixture of rapidly equilibrating monomeric conformers which, on average, contain little secondary structure and no hydrophobic core. This conclusion is based on spectroscopic and hydrodynamic probes of protein structure, as well as the behavior of the protein in the presence of additives and cosolvents.
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: disorder (Structural state)
Evidence: spectrometry evidence used in manual assertion
Supporting statements:
Circular dichroism (CD) and Fourier-transform infrared spectroscopy (FTIR) indicate the absence of significant amounts of secondary structure in NACP, while CD and ultraviolet spectroscopy suggest the lack of a hydrophobic core.
CD, UV, and FTIR Spectroscopy Indicate NACP Has a “Random Coil” Conformation.
These features indicate that NACP exists as a mixture of rapidly equilibrating extended conformers and is representative of a class of "natively unfolded" proteins, many of which potentiate protein-protein interactions.
NACP Is a “Natively Unfolded” Protein. The results presented herein provide evidence that, in solution, NACP exists as a mixture of rapidly equilibrating monomeric conformers which, on average, contain little secondary structure and no hydrophobic core. This conclusion is based on spectroscopic and hydrodynamic probes of protein structure, as well as the behavior of the protein in the presence of additives and cosolvents.
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 140
Annotation: disorder (Structural state)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
Circular dichroism (CD) and Fourier-transform infrared spectroscopy (FTIR) indicate the absence of significant amounts of secondary structure in NACP, while CD and ultraviolet spectroscopy suggest the lack of a hydrophobic core.
CD, UV, and FTIR Spectroscopy Indicate NACP Has a “Random Coil” Conformation.
These features indicate that NACP exists as a mixture of rapidly equilibrating extended conformers and is representative of a class of "natively unfolded" proteins, many of which potentiate protein-protein interactions.
NACP Is a “Natively Unfolded” Protein. The results presented herein provide evidence that, in solution, NACP exists as a mixture of rapidly equilibrating monomeric conformers which, on average, contain little secondary structure and no hydrophobic core. This conclusion is based on spectroscopic and hydrodynamic probes of protein structure, as well as the behavior of the protein in the presence of additives and cosolvents.
Protein: DP00070 (UniProt P37840)
Region: residues 61	to 95
Annotation: amyloid fibril formation (Biological process)
Evidence: circular dichroism evidence used in manual assertion
Supporting statements:
The “non-Aβ component of Alzheimer's disease amyloid plaque” (NAC) is a minor peptide component of the insoluble fibrillar core of the Alzheimer's disease (AD) neuritic plaque. NAC amyloid fibrils seed the polymerization of Aβ1−40, the major AD amyloid protein. NAC is derived from a 14 kDa precursor protein, designated NACP, a member of a highly conserved family of heat-stable brain-specific acidic proteins which have been suggested to be involved in synapse formation and/or stabilization.
This behavior suggests that NAC amyloid may accelerate AD amyloidogenesis by seeding in vivo plaque formation (Han et al., 1995). 
NAC is indicated with bold lettering, and the other peptides used in this work (NACP19−48 and NACP96−125) are underlined.
In contrast to the spectra of the other two peptides, the CD spectrum of a saturated solution (11 μM) of the NAC peptide (NACP61−95) in aqueous buffer indicated a significant degree of β-sheet structure (ca. 35% β, Figure 3B). Similar CD spectra have been measured for aqueous solutions of Aβ amyloid peptides (Barrow & Zagorski, 1991).
Protein: DP00070 (UniProt P37840)
Region: residues 1	to 102
Annotation: lipid binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
CD data (Figure 4) confirm that αS undergoes a large conformational transition to an α-helical state in the presence of SDS micelles, as it does in the presence of lipid vesicles, confirming that the protein interacts with the micelles, possibly in a similar fashion.
Far-UV CD data from wild-type αS in the presence and absence of SDS micelles, under conditions and protein concentrations (100 μM) identical to those used in the NMR experiments. A large conformational change is evident, with a high degree of helicity (indicated by the characteristic double minima at 208 and 222 nm) formed in the presence of micelles.
Lipid vesicles were prepared by mixing equal amounts of freshly procured 1-palmitoyl 2-oleoyl PC and PA in chloroform (Avanti Polar Lipids).