Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
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Antibody Binding Modulates Conformational Exchange in Domain III of Dengue Virus E ProteinFunctional role of transient conformations: Rediscovering "chronosteric effects" thirty years laterA Combinatorial NMR and EPR Approach for Evaluating the Structural Ensemble of Partially Folded ProteinsCold denaturation of a protein dimer monitored at atomic resolutionWhen fast is better: protein folding fundamentals and mechanisms from ultrafast approachesStudying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to BiomoleculesElectrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formationInsights into the folding and unfolding processes of wild-type and mutated SH3 domain by molecular dynamics and replica exchange molecular dynamics simulations.Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.NMR approaches in structure-based lead discovery: recent developments and new frontiers for targeting multi-protein complexesIntegrative structure modeling of macromolecular assemblies from proteomics dataPartially folded equilibrium intermediate of the villin headpiece HP67 defined by 13C relaxation dispersion.Fast protein folding kineticsProtein vivisection reveals elusive intermediates in foldingCONNJUR spectrum translator: an open source application for reformatting NMR spectral data.Visualizing transient dark states by NMR spectroscopy.Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.An introduction to NMR-based approaches for measuring protein dynamics.Structure of an intermediate conformer of the spindle checkpoint protein Mad2Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopyConformational dynamics of a G-protein α subunit is tightly regulated by nucleotide binding.Protein folding on the ribosome studied using NMR spectroscopy.The folding of single domain proteins--have we reached a consensus?Examining the relationship between RNA function and motion using nuclear magnetic resonance.Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy.The dynamic duo: combining NMR and small angle scattering in structural biology.Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion.Modeling of proteins and their assemblies with the Integrative Modeling Platform.Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments.Enhanced accuracy of kinetic information from CT-CPMG experiments by transverse rotating-frame spectroscopy.Pressure dependence of side chain 13C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH2.The low populated folding intermediate of a mutant of the Fyn SH3 domain identified by a simple model.
P2860
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P2860
Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
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2009 nî lūn-bûn
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2009 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մարտին հրատարակված գիտական հոդված
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2009年の論文
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2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
@ast
Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
@en
type
label
Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
@ast
Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
@en
prefLabel
Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
@ast
Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
@en
P2860
P1433
P1476
Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
@en
P2093
Patrik Lundström
P2860
P304
P356
10.1016/J.BPJ.2008.12.3907
P407
P577
2009-03-01T00:00:00Z