cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5281/zenodo.18780842
title: INTERNATIONAL TRADE AND POVERTY REDUCTION IN NIGERIA, 2019 - 2024

description: This study examines the impact of international trade on poverty reduction in Nigeria between 2019 and 2024, with particular emphasis on trade diversification in non-oil sectors such as agriculture and manufacturing. Nigeria’s heavy dependence on crude oil exports has continued to expose the economy to external shocks, limiting inclusive growth and effective poverty reduction. Against this backdrop, the study adopts a quantitative survey research design to assess how trade diversification, infrastructural development, and social protection measures influence poverty outcomes in Nigeria. Data were collected from 400 respondents using a structured questionnaire and analyzed through descriptive statistics and chi-square techniques. The study is anchored on the Trade and Development Theory and Dependency Theory, which provide a theoretical basis for understanding the role of international trade in development and structural inequality in developing economies. The findings reveal strong public support for trade diversification as a critical pathway for poverty reduction, employment generation and sustainable national development. The results further indicate that improvements in infrastructure significantly enhance Nigeria’s participation in international trade, while effective social protection measures play a vital role in ensuring that trade benefits are equitably distributed, particularly among vulnerable populations.The study concludes that international trade can contribute meaningfully to poverty reduction in Nigeria when it is supported by diversified non-oil exports, adequate infrastructure, and inclusive social protection frameworks. However, without deliberate policies to address structural constraints and inequality, the poverty-reducing potential of trade remains limited. Based on these conclusions and findings, the study recommends sustained investment in agriculture and manufacturing, improved infrastructural development, expansion of social protection programmes, and the adoption of inclusive trade and economic policies to ensure equitable distribution of trade benefits and long-term national transformation.
DOI: 10.5281/zenodo.18780843
title: INTERNATIONAL TRADE AND POVERTY REDUCTION IN NIGERIA, 2019 - 2024

description: This study examines the impact of international trade on poverty reduction in Nigeria between 2019 and 2024, with particular emphasis on trade diversification in non-oil sectors such as agriculture and manufacturing. Nigeria’s heavy dependence on crude oil exports has continued to expose the economy to external shocks, limiting inclusive growth and effective poverty reduction. Against this backdrop, the study adopts a quantitative survey research design to assess how trade diversification, infrastructural development, and social protection measures influence poverty outcomes in Nigeria. Data were collected from 400 respondents using a structured questionnaire and analyzed through descriptive statistics and chi-square techniques. The study is anchored on the Trade and Development Theory and Dependency Theory, which provide a theoretical basis for understanding the role of international trade in development and structural inequality in developing economies. The findings reveal strong public support for trade diversification as a critical pathway for poverty reduction, employment generation and sustainable national development. The results further indicate that improvements in infrastructure significantly enhance Nigeria’s participation in international trade, while effective social protection measures play a vital role in ensuring that trade benefits are equitably distributed, particularly among vulnerable populations.The study concludes that international trade can contribute meaningfully to poverty reduction in Nigeria when it is supported by diversified non-oil exports, adequate infrastructure, and inclusive social protection frameworks. However, without deliberate policies to address structural constraints and inequality, the poverty-reducing potential of trade remains limited. Based on these conclusions and findings, the study recommends sustained investment in agriculture and manufacturing, improved infrastructural development, expansion of social protection programmes, and the adoption of inclusive trade and economic policies to ensure equitable distribution of trade benefits and long-term national transformation.
DOI: 10.13018/bmr2329
title: Structural determinants of Cys2His2 zinc fingers
DOI: 10.13018/bmr2331
title: Individual Assignments of the Amide Proton Resonances Involved in the Triple-Stranded Antiparallel Pleated beta-Sheet Structure of a Long Neurotoxin, Laticauda Semifasciata III from Laticauda semifasciata
DOI: 10.13018/bmr2338
title: A Two-Dimensional NMR Method for Assignment of Imidazole Ring Proton Resonances of Histidine Residues in Proteins
DOI: 10.13018/bmr2345
title: Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins
DOI: 10.13018/bmr2346
title: Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins
DOI: 10.13018/bmr2347
title: Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins
DOI: 10.34740/kaggle/dsv/14966253
title: World Weather Repository ( Daily Updating )
DOI: 10.13018/bmr2348
title: Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins
DOI: 10.13018/bmr2352
title: Structural and Electronic Properties of the Liver Fluke Heme Cavity by Nuclear Magnetic Resonance and Optical Spectroscopy. Evidence for a Distal Tyrosine Residue in a Normally Functioning Hemoglobin.
DOI: 10.13018/bmr2353
title: 15N nuclear magnetic resonance studies of the B domain of Staphylococcal protein A: Sequence specific assignments of the imide 15N resonances of the proline residues and the interaction with human immunoglobin G
DOI: 10.13018/bmr2366
title: Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c
DOI: 10.13018/bmr2367
title: Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c
DOI: 10.13018/bmr2368
title: Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c
DOI: 10.13018/bmr2371
title: Three-Dimensional 15N-1H-1H and 15N-13C-1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli
DOI: 10.13018/bmr2384
title: 1H NMR-Based Determination of the Secondary Structure of Porcine Pancreatic Spasmolytic Polypeptide: One of a New Family of "Trefoil" Motif Containing Cell Growth Factors
DOI: 10.13018/bmr2395
title: Location of an alpha-Helix in Fragment 96-133 from Bovine Somatotropin by 1H NMR Spectroscopy
DOI: 10.13018/bmr2396
title: Mapping the Substrate-Binding Site of a Human Class Mu Glutathione Transferase Using Nuclear Magnetic Resonance Spectroscopy
DOI: 10.13018/bmr2410
title: Sequence-specific 1H, 15N, and 13C assignment of the N-terminal domain of the human oncoprotein MDM2 that binds to p53
DOI: 10.13018/bmr2425
title: Nature and Locations of the Most Slowly Exchanging Peptide NH Protons in Residues 1 to 19 of Ribonuclease S
DOI: 10.13018/bmr2426
title: Nature and Locations of the Most Slowly Exchanging Peptide NH Protons in Residues 1 to 19 of Ribonuclease S
DOI: 10.13018/bmr2431
title: Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements
DOI: 10.13018/bmr2432
title: Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements
DOI: 10.13018/bmr2433
title: Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements
DOI: 10.13018/bmr2434
title: Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements
DOI: 10.13018/bmr2435
title: Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
DOI: 10.13018/bmr2436
title: Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
DOI: 10.13018/bmr2437
title: Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
DOI: 10.13018/bmr2438
title: Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
DOI: 10.13018/bmr2439
title: Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
DOI: 10.13018/bmr2440
title: Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
DOI: 10.13018/bmr2442
title: Nucleotide Binding and GTP Hydrolysis by Elongation Factor Tu from Thermus thermophilus As Monitored by Proton NMR
DOI: 10.13018/bmr2443
title: Nucleotide Binding and GTP Hydrolysis by Elongation Factor Tu from Thermus thermophilus As Monitored by Proton NMR
DOI: 10.13018/bmr2446
title: Studies of beta-Sheet Structure in Lysozyme by Proton Nuclear Magnetic Resonance. Assignments and Analysis of Spin-Spin Coupling Constants
DOI: 10.13018/bmr2454
title: Acyl Carrier Protein from Escherichia coli I. Aspects of the Solution Structure As Evidenced by Proton Nuclear Overhauser Experiments at 500 MHz
DOI: 10.15468/dl.k6sj6h
title: Occurrence Download

description: A dataset containing 66 species occurrences available in GBIF matching the query:
{
 "and" : [
 "Country is Uzbekistan",
 "TaxonKey is Nitrariaceae"
 ]
}

 The dataset includes 66 records from 5 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0002729-260225131425191/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.13018/bmr2455
title: pH and Temperature Effects on the Molecular Conformation of the Porcine Pancreatic Secretory Trypsin Inhibitor As Detected by Hydrogen-1 Nuclear Magnetic Resonance
DOI: 10.13018/bmr2457
title: Preliminary Structural Comparison of the Proteinase Isoinhibitors IIA and IIB from Bull Seminal Plasma Based on Individual Assignments of the 1H Nuclear Magnetic Resonance Spectra by Two-dimensional Nuclear Magnetic Resonance at 500 MHz
DOI: 10.13018/bmr2463
title: Heternuclear (1H,13C) Two-Dimensional Chemical Shift Correlation NMR Spectroscopy of a Protein. Ferredoxin from Anabaena variabilis
DOI: 10.13018/bmr2472
title: 1H NMR Studies of a Two-Iron: Two-Sulfur Ferredoxin from Halobacterium of the Dead Sea
DOI: 10.13018/bmr2473
title: Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy
DOI: 10.13018/bmr2474
title: Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy
DOI: 10.13018/bmr2475
title: Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy
DOI: 10.13018/bmr2476
title: A Proton NMR and Nuclear Overhauser Effect (NOE) Study of Human Plasma Prealbumin, Including the Development and Application to Spectral Assignment of a Combined Ring Current Shift and NOE Prediction Program
DOI: 10.13018/bmr2488
title: Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect
DOI: 10.13018/bmr2489
title: Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect
DOI: 10.13018/bmr2498
title: 1H-NMR Assignment and Secondary structure of Human Insulin-Like Growth Factor-I (IGF-I) in Solution
DOI: 10.13018/bmr2506
title: Heteronuclear Three-Dimensional NMR Spectroscopy of the Inflammatory Protein C5a
DOI: 10.15468/dl.huqup8
title: Occurrence Download

description: A dataset containing 215 species occurrences available in GBIF matching the query:
{
 "and" : [
 "GadmGid is CHN.29_1",
 "HasCoordinate is true",
 "HasGeospatialIssue is false",
 "OccurrenceStatus is Present",
 "TaxonKey is Dicaeum ignipectus"
 ]
}

 The dataset includes 215 records from 3 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0002730-260225131425191/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.13018/bmr2512
title: pH-Dependent Properties of Cobalt(II) Carboxypeptidase A-Inhibitor Complexes
DOI: 10.13018/bmr2513
title: pH-Dependent Properties of Cobalt(II) Carboxypeptidase A-Inhibitor Complexes
DOI: 10.13018/bmr2527
title: Two-Dimensional NMR Studies of Squash Family Inhibitors. Sequence-Specific Proton Assignments and Secondary Structure of Reactive-Site Hydrolyzed Cucurbita maxima Trypsin Inhibitor III
DOI: 10.13018/bmr2528
title: Conformation and Dynamics of an Fab'-Bound Peptide by Isotope-Edited NMR Spectroscopy
DOI: 10.13018/bmr2529
title: Conformation and Dynamics of an Fab'-Bound Peptide by Isotope-Edited NMR Spectroscopy
DOI: 10.13018/bmr2539
title: Determination of the Nuclear Magnetic Resonance Solution Structure of the DNA-binding Domain (Residues 1 to 69) of the 434 Repressor and Comparison with the X-ray Crystal Structure
DOI: 10.13018/bmr2542
title: 1H and 15N NMR Study of Human Lysozyme
DOI: 10.13018/bmr2546
title: Three-Dimensional Solution Structure of the E3-Binding Domain of the Dihydrolipoamide Succinyltransferase Core from the 2-Oxoglutarate Dehydrogenase Multienzyme Complex of Escherichia coli
DOI: 10.13018/bmr2547
title: Three-Dimensional Solution Structure of the E3-Binding Domain of the Dihydrolipoamide Succinyltransferase Core from the 2-Oxoglutarate Dehydrogenase Multienzyme Complex of Escherichia coli
DOI: 10.13018/bmr2573
title: Fast Internal Main-Chain Dynamics of Human Ubiquitin
DOI: 10.13018/bmr2574
title: Fast Internal Main-Chain Dynamics of Human Ubiquitin
DOI: 10.13018/bmr2575
title: Sequence-Specific 1H NMR Assignments and Secondary Structure of the Streptococcal Protein G B2-Domain
DOI: 10.13018/bmr2580
title: Sequence-specific resonance assignment and secondary structure of (1-71) bacterioopsin
DOI: 10.13018/bmr2590
title: Transmembrane Region of Wild-type and Mutant M13 Coat Proteins Conformational Role of beta-Branched Residues
DOI: 10.15468/dl.3bqxcp
title: Occurrence Download

description: A dataset containing 244 species occurrences available in GBIF matching the query:
{
 "and" : [
 "HasGeospatialIssue is false",
 "HasCoordinate is true",
 "OccurrenceStatus is Present",
 {
 "not" : {
 "BasisOfRecord" : [
 "is one of (Fossil, Living Specimen)"
 ]
 }
 },
 "DistanceFromCentroidInMeters is greater than or equal to 2000",
 "Geometry POLYGON ((105.610544 14.999999, 179.999961 14.999999, 179.999961 65.08290100000001, 105.610544 65.08290100000001, 105.610544 14.999999))",
 "TaxonKey is Dascyllus aruanus"
 ]
}

 The dataset includes 244 records from 23 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0002731-260225131425191/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.13018/bmr2591
title: Transmembrane Region of Wild-type and Mutant M13 Coat Proteins Conformational Role of beta-Branched Residues
DOI: 10.13018/bmr2592
title: Transmembrane Region of Wild-type and Mutant M13 Coat Proteins Conformational Role of beta-Branched Residues
DOI: 10.13018/bmr2606
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2607
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2608
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2609
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2610
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2611
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2612
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2613
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2614
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2615
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.15468/dl.w55qve
title: Occurrence Download

description: A dataset containing 5 species occurrences available in GBIF matching the query:
{
 "TaxonKey" : [
 "is Trimeresurus gunaleni"
 ]
}

 The dataset includes 5 records from 1 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0002732-260225131425191/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.13018/bmr2616
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2617
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2618
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2619
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2620
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2621
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2622
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2623
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.15468/dl.nswhp5
title: Occurrence Download

description: A dataset containing 10 species occurrences available in GBIF matching the query:
{
 "TaxonKey" : [
 "is Trimeresurus fasciatus"
 ]
}

 The dataset includes 10 records from 6 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0002733-260225131425191/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.13018/bmr2624
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2625
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2627
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2628
title: Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes
DOI: 10.13018/bmr2630
title: Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escherichia coli
DOI: 10.13018/bmr2631
title: Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escherichia coli
DOI: 10.15468/dl.7e3n3m
title: Occurrence Download

description: A dataset containing 329 species occurrences available in GBIF matching the query:
{
 "and" : [
 "Country is India",
 "OccurrenceStatus is Present",
 "TaxonKey is Terminalia chebula",
 "Year 2000-2026"
 ]
}

 The dataset includes 329 records from 11 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0002734-260225131425191/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.13018/bmr2632
title: Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escherichia coli
DOI: 10.13018/bmr2638
title: 1H NMR and UV-Vis Spectroscopic Characterization of Sulfonamide Complexes of Nickel(II)-Carbonic Anhydrase. Resonance Assignments Based on NOE Effects
DOI: 10.13018/bmr2639
title: 1H NMR and UV-Vis Spectroscopic Characterization of Sulfonamide Complexes of Nickel(II)-Carbonic Anhydrase. Resonance Assignments Based on NOE Effects
DOI: 10.13018/bmr2640
title: 1H NMR and UV-Vis Spectroscopic Characterization of Sulfonamide Complexes of Nickel(II)-Carbonic Anhydrase. Resonance Assignments Based on NOE Effects
DOI: 10.13018/bmr2641
title: 1H NMR and UV-Vis Spectroscopic Characterization of Sulfonamide Complexes of Nickel(II)-Carbonic Anhydrase. Resonance Assignments Based on NOE Effects
DOI: 10.13018/bmr2642
title: 1H NMR and UV-Vis Spectroscopic Characterization of Sulfonamide Complexes of Nickel(II)-Carbonic Anhydrase. Resonance Assignments Based on NOE Effects
DOI: 10.13018/bmr2651
title: Site-Directed Mutagenesis and 1H NMR Spectroscopy of an Interdomain Segment in the Pyruvate Dehydrogenase Multienzyme Complex of Escherichia coli
DOI: 10.13018/bmr2652
title: Hydrogen-Exchange Kinetics of the Indole NH Proton of the Buried Tryptophan in the Constant Fragment of the Immunoglobulin Light Chain
DOI: 10.13018/bmr2707
title: Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins
DOI: 10.13018/bmr2708
title: Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins
DOI: 10.13018/bmr2709
title: Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins
DOI: 10.13018/bmr2710
title: Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins
DOI: 10.13018/bmr2711
title: Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins
DOI: 10.13018/bmr2712
title: Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins
DOI: 10.13018/bmr2718
title: A 1H-NMR study of human interleukin-1beta Sequence-specific assignment of aromatic residues using site-directed mutant proteins
DOI: 10.13018/bmr2719
title: A 1H-NMR study of human interleukin-1beta Sequence-specific assignment of aromatic residues using site-directed mutant proteins
DOI: 10.13018/bmr2763
title: Comparison of the Structure and Dynamics of Chicken Gizzard and Rabbit Cardiac Tropomyosins: 1H NMR Spectroscopy and Measurement of Amide Hydrogen Exchange Rates
DOI: 10.13018/bmr2764
title: NMR studies of the trp repressor from Escherichia coli Characterisation and assignments of residue types
DOI: 10.13018/bmr2768
title: Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
DOI: 10.13018/bmr2784
title: Dynamics of Methyl Groups in Proteins As Studied by Proton-Detected 13C NMR Spectroscopy. Application to the Leucine Residues of Staphylococcal Nuclease