How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?
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Recommendations of the wwPDB NMR Validation Task ForcePrinciples and Overview of Sampling Methods for Modeling Macromolecular Structure and DynamicsSolution Structure of Alg13: The Sugar Donor Subunit of a Yeast N-Acetylglucosamine TransferaseSolution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and Its 146 kDa Complex with HPr Using Residual Dipolar Couplings and Small- and Wide-Angle X-ray ScatteringWeak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular RecognitionSolution Structure of CCP Modules 10–12 Illuminates Functional Architecture of the Complement Regulator, Factor HThe catalytic domain of MMP-1 studied through tagged lanthanidespH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMRStructures of the Excited States of Phospholamban and Shifts in Their Populations upon PhosphorylationDetermination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplingsSpatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEsIntegrative, dynamic structural biology at atomic resolution--it's about timeUsing small angle solution scattering data in Xplor-NIH structure calculationsCorrelated inter-domain motions in adenylate kinaseMulti-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamicsDynamics may significantly influence the estimation of interatomic distances in biomolecular X-ray structuresAssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra.Simultaneous determination of protein structure and dynamics.Quality assessment of protein NMR structures.Protein NMR structures refined with Rosetta have higher accuracy relative to corresponding X-ray crystal structuresEnsemble MD simulations restrained via crystallographic data: accurate structure leads to accurate dynamicsSelf-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics.Structural biology by NMR: structure, dynamics, and interactions.Using the experimentally determined components of the overall rotational diffusion tensor to restrain molecular shape and size in NMR structure determination of globular proteins and protein-protein complexes.Toward a unified representation of protein structural dynamics in solution.Ways and means of coping with uncertainties of the relationship of the genetic blue print to protein structure and function in the cellThe use of residual dipolar coupling in studying proteins by NMR.Cyclophilin A catalyzes proline isomerization by an electrostatic handle mechanism.Information content of long-range NMR data for the characterization of conformational heterogeneity.A critical assessment of methods to recover information from averaged data.Residual dipolar coupling measurements of transmembrane proteins using aligned low-q bicelles and high-resolution magic angle spinning NMR spectroscopy.Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.In silico elucidation of the recognition dynamics of ubiquitinStructural dynamics of bio-macromolecules by NMR: the slowly relaxing local structure approachIdentification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings.Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase systemA relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synucleinVisualizing transient dark states by NMR spectroscopy.Relation between native ensembles and experimental structures of proteins.Estimation of interdomain flexibility of N-terminus of factor H using residual dipolar couplings
P2860
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P2860
How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?
description
2004 nî lūn-bûn
@nan
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
How much backbone motion in ub ...... independent cross-validation?
@ast
How much backbone motion in ub ...... independent cross-validation?
@en
type
label
How much backbone motion in ub ...... independent cross-validation?
@ast
How much backbone motion in ub ...... independent cross-validation?
@en
prefLabel
How much backbone motion in ub ...... independent cross-validation?
@ast
How much backbone motion in ub ...... independent cross-validation?
@en
P356
P1476
How much backbone motion in ub ...... independent cross-validation?
@en
P2093
G Marius Clore
P304
P356
10.1021/JA0386804
P407
P577
2004-03-01T00:00:00Z