Insights into the local residual entropy of proteins provided by NMR relaxation.
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Correlation as a determinant of configurational entropy in supramolecular and protein systemsThe ensemble nature of allosteryNMR insights into protein allosteryProtein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow β-sheet motionsDistance-Based Configurational Entropy of Proteins from Molecular Dynamics SimulationsTheory of free energy and entropy in noncovalent bindingConfigurational entropy in protein-peptide binding: computational study of Tsg101 ubiquitin E2 variant domain with an HIV-derived PTAP nonapeptideOn the relationship between NMR-derived amide order parameters and protein backbone entropy changesUltrafast NMR T1 relaxation measurements: probing molecular properties in real timeQuantitative comparison of errors in 15N transverse relaxation rates measured using various CPMG phasing schemesFlexible backbone sampling methods to model and design protein alternative conformationsChanging the topology of protein backbone: the effect of backbone cyclization on the structure and dynamics of a SH3 domain.The response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinaseInternal dynamics of dynactin CAP-Gly is regulated by microtubules and plus end tracking protein EB1.Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics.Conformational dynamics and thermodynamics of protein-ligand binding studied by NMR relaxation.Protein activity regulation by conformational entropy.Quantitative observation of backbone disorder in native elastin.Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer DataAccurate determination of rates from non-uniformly sampled relaxation data.The physical basis of model-free analysis of NMR relaxation data from proteins and complex fluids.A surprising role for conformational entropy in protein function.Ligand-induced changes in the structure and dynamics of Escherichia coli peptide deformylaseStructural dynamics of bio-macromolecules by NMR: the slowly relaxing local structure approachConformational entropy in molecular recognition by proteins.Dynamic multidrug recognition by multidrug transcriptional repressor LmrR.Modeling loop entropy.The role of conformational entropy in molecular recognition by calmodulin.Backbone dynamics of deoxy and carbonmonoxy hemoglobin by NMR/SRLS.Exposing the Moving Parts of Proteins with NMR Spectroscopy.Protein-Inhibitor Interaction Studies Using NMRProbing the binding entropy of ligand-protein interactions by NMR.15N backbone dynamics of the S-peptide from ribonuclease A in its free and S-protein bound forms: toward a site-specific analysis of entropy changes upon foldingThe role of backbone conformational heat capacity in protein stability: temperature dependent dynamics of the B1 domain of Streptococcal protein G.Entropy in molecular recognition by proteins.Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution.The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation.Using NMR spectroscopy to elucidate the role of molecular motions in enzyme functionConformational contribution to thermodynamics of binding in protein-peptide complexes through microscopic simulation
P2860
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P2860
Insights into the local residual entropy of proteins provided by NMR relaxation.
description
1996 nî lūn-bûn
@nan
1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
name
Insights into the local residual entropy of proteins provided by NMR relaxation.
@ast
Insights into the local residual entropy of proteins provided by NMR relaxation.
@en
type
label
Insights into the local residual entropy of proteins provided by NMR relaxation.
@ast
Insights into the local residual entropy of proteins provided by NMR relaxation.
@en
prefLabel
Insights into the local residual entropy of proteins provided by NMR relaxation.
@ast
Insights into the local residual entropy of proteins provided by NMR relaxation.
@en
P2093
P2860
P356
P1433
P1476
Insights into the local residual entropy of proteins provided by NMR relaxation.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560051228
P577
1996-12-01T00:00:00Z