Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy.
about
Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein foldingA transient and low-populated protein-folding intermediate at atomic resolutionCold denaturation of a protein dimer monitored at atomic resolutionMapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.A residue in helical conformation in the native state adopts a β-strand conformation in the folding transition state despite its high and canonical Φ-value.The redundancy of NMR restraints can be used to accelerate the unfolding behavior of an SH3 domain during molecular dynamics simulationsMutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.Protein folding and misfolding: mechanism and principles.Chemical exchange in biomacromolecules: past, present, and future.Joint non-uniform sampling of all incremented time delays for quicker acquisition in protein relaxation studies.Visualizing transient dark states by NMR spectroscopy.Roles of beta-turns in protein folding: from peptide models to protein engineering.NMR spectroscopy brings invisible protein states into focus.What lessons can be learned from studying the folding of homologous proteins?Transient non-native hydrogen bonds promote activation of a signaling protein.Understanding the mechanism of prosegment-catalyzed folding by solution NMR spectroscopy.Widespread transient Hoogsteen base pairs in canonical duplex DNA with variable energeticsThe mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints.Evidence against the "Y-T coupling" mechanism of activation in the response regulator NtrC.The low populated folding intermediate of a mutant of the Fyn SH3 domain identified by a simple model.
P2860
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P2860
Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy.
description
2007 nî lūn-bûn
@nan
2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Phi-value analysis of a three- ...... ation dispersion spectroscopy.
@ast
Phi-value analysis of a three- ...... ation dispersion spectroscopy.
@en
type
label
Phi-value analysis of a three- ...... ation dispersion spectroscopy.
@ast
Phi-value analysis of a three- ...... ation dispersion spectroscopy.
@en
prefLabel
Phi-value analysis of a three- ...... ation dispersion spectroscopy.
@ast
Phi-value analysis of a three- ...... ation dispersion spectroscopy.
@en
P2860
P50
P356
P1476
Phi-value analysis of a three- ...... ation dispersion spectroscopy.
@en
P2093
Alan R Davidson
P2860
P304
15717-15722
P356
10.1073/PNAS.0705097104
P407
P577
2007-09-26T00:00:00Z