Long-range order in the src SH3 folding transition state
about
Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein foldingInsights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free waterConstructing sequence-dependent protein models using coevolutionary information.Changing the topology of protein backbone: the effect of backbone cyclization on the structure and dynamics of a SH3 domain.Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formationPropensity to form amyloid fibrils is encoded as excitations in the free energy landscape of monomeric proteins.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.Kinetic consequences of native state optimization of surface-exposed electrostatic interactions in the Fyn SH3 domain.The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition 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.Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.Transition states for protein folding have native topologies despite high structural variability.Formation of the folding nucleus of an SH3 domain investigated by loosely coupled molecular dynamics simulations.Direct molecular dynamics observation of protein folding transition state ensembleMolecular dynamics simulations of protein folding from the transition state.Molecular dynamics simulations of a highly charged peptide from an SH3 domain: possible sequence-function relationship.Searching for folded proteins in vitro and in silico.Planning combinatorial disulfide cross-links for protein fold determination.Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformationLong range Trp-Trp interaction initiates the folding pathway of a pro-angiogenic β-hairpin peptideEarly turn formation and chain collapse drive fast folding of the major cold shock protein CspA of Escherichia coli.Multi-state proteins: approach allowing experimental determination of the formation order of structure elements in the green fluorescent protein.Collapse kinetics and chevron plots from simulations of denaturant-dependent folding of globular proteins.The topomer search model: A simple, quantitative theory of two-state protein folding kinetics.Dynamics of an ultrafast folding subdomain in the context of a larger protein fold.Tightening up the structure, lighting up the pathway: Application of molecular constraints and light to manipulate protein folding, self-assembly and function.The H2A-H2B dimeric kinetic intermediate is stabilized by widespread hydrophobic burial with few fully native interactions.Spider wrapping silk fibre architecture arising from its modular soluble protein precursor.Mutational effects on the folding dynamics of a minimized hairpin.Assessment of local friction in protein folding dynamics using a helix cross-linker.How quickly can a β-hairpin fold from its transition state?Hydration of the folding transition state ensemble of a protein.Intramolecular cross-linking evaluated as a structural probe of the protein folding transition state.A "Link-Psi" strategy using crosslinking indicates that the folding transition state of ubiquitin is not very malleable.A cross-strand Trp Trp pair stabilizes the hPin1 WW domain at the expense of function.Low energy pathways and non-native interactions: the influence of artificial disulfide bridges on the mechanism of folding.Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c.Folding behavior of ribosomal protein S6 studied by modified Gō-like model.Simplified protein models: predicting folding pathways and structure using amino acid sequences.
P2860
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P2860
Long-range order in the src SH3 folding transition state
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Long-range order in the src SH3 folding transition state
@ast
Long-range order in the src SH3 folding transition state
@en
type
label
Long-range order in the src SH3 folding transition state
@ast
Long-range order in the src SH3 folding transition state
@en
prefLabel
Long-range order in the src SH3 folding transition state
@ast
Long-range order in the src SH3 folding transition state
@en
P2860
P356
P1476
Long-range order in the src SH3 folding transition state
@en
P2093
D S Riddle
V P Grantcharova
P2860
P304
P356
10.1073/PNAS.97.13.7084
P407
P50
P577
2000-06-01T00:00:00Z