The folding kinetics and thermodynamics of the Fyn-SH3 domain.
about
Obligatory steps in protein folding and the conformational diversity of the transition stateThe peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction.On the precision of experimentally determined protein folding rates and phi-valuesA partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited foldingSolution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP.Turbulent phenomena in protein folding.Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.Structure, stability, and flexibility of ribosomal protein L14e from Sulfolobus solfataricusRelaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state.Sparsely populated folding intermediates of the Fyn SH3 domain: matching native-centric essential dynamics and experimentLow-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.Detection and characterization of partially unfolded oligomers of the SH3 domain of alpha-spectrin.A binding event converted into a folding event.The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysisThe identification of conserved interactions within the SH3 domain by alignment of sequences and structures.Structural events during the refolding of an all beta-sheet protein.Long-range order in the src SH3 folding transition stateImportant role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain.Amyloid fibril formation by an SH3 domain.Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformationProtein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.Coupling between properties of the protein shape and the rate of protein folding.beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallinEngineering a signal transduction mechanism for protein-based biosensors.Ultrafast folding of alpha3D: a de novo designed three-helix bundle proteinThe topomer-sampling model of protein foldingLabel-Free SERS Detection of Small Proteins Modified to Act as Bifunctional Linkers.Probing the protein-folding mechanism using denaturant and temperature effects on rate constantsDynameomics: a consensus view of the protein unfolding/folding transition state ensemble across a diverse set of protein folds.Random-coil behavior and the dimensions of chemically unfolded proteins.NMR spectroscopy brings invisible protein states into focus.Non-sequence-specific interactions can account for the compaction of proteins unfolded under "native" conditions.Evidence for the principle of minimal frustration in the evolution of protein folding landscapes.Contact order revisited: influence of protein size on the folding rate.Optimal region of average side-chain entropy for fast protein foldingCooperativity and the origins of rapid, single-exponential kinetics in protein folding.Spatial ranges of driving forces are a key determinant of protein folding cooperativity and rate diversity.Integrated prediction of protein folding and unfolding rates from only size and structural class.
P2860
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P2860
The folding kinetics and thermodynamics of the Fyn-SH3 domain.
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The folding kinetics and thermodynamics of the Fyn-SH3 domain.
@ast
The folding kinetics and thermodynamics of the Fyn-SH3 domain.
@en
type
label
The folding kinetics and thermodynamics of the Fyn-SH3 domain.
@ast
The folding kinetics and thermodynamics of the Fyn-SH3 domain.
@en
prefLabel
The folding kinetics and thermodynamics of the Fyn-SH3 domain.
@ast
The folding kinetics and thermodynamics of the Fyn-SH3 domain.
@en
P2093
P356
P1433
P1476
The folding kinetics and thermodynamics of the Fyn-SH3 domain
@en
P2093
Campbell ID
Guijarro JI
Pitkeathly M
P304
P356
10.1021/BI972075U
P407
P577
1998-02-01T00:00:00Z