Extremely rapid protein folding in the absence of intermediates.
about
RNA single strands bind to a conserved surface of the major cold shock protein in crystals and solutionObligatory steps in protein folding and the conformational diversity of the transition stateExamination of the folding of E. coli CspA through tryptophan substitutionsMultiple unfolding intermediates of human placental alkaline phosphatase in equilibrium urea denaturationA partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited foldingCold shock stress-induced proteins in Bacillus subtilisUnusual dimerization of a BcCsp mutant leads to reduced conformational dynamics.Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase complex.Cloning, overexpression, purification, and physicochemical characterization of a cold shock protein homolog from the hyperthermophilic bacterium Thermotoga maritima.The trehalose coating effect on the internal protein dynamics.Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxideProtein folding and unfolding on a complex energy landscape.Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspBMicrosecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.A speed limit for conformational change of an allosteric membrane protein.Fast protein folding kineticsElementary steps in protein folding.Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.Influence of the stability of a fused protein and its distance to the amyloidogenic segment on fibril formation.Surfing on protein folding energy landscapes.Early turn formation and chain collapse drive fast folding of the major cold shock protein CspA of Escherichia coli.Folding pathway of a lattice model for proteins.Protein folding and unfolding in microseconds to nanoseconds by experiment and simulationStructure and function of cold shock proteins in archaea.Submillisecond protein folding kinetics studied by ultrarapid mixing.Diffusion control in an elementary protein folding reaction.Transient aggregates in protein folding are easily mistaken for folding intermediates.Mutational analysis of the BPTI folding pathway: I. Effects of aromatic-->leucine substitutions on the distribution of folding intermediatesAbsence of a stable intermediate on the folding pathway of protein A.Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force.Cytochrome c folds through a smooth funnelOrigins of barriers and barrierless folding in BBL.The speed limit for protein folding measured by triplet-triplet energy transfer.Single-molecule fluorescence studies of protein folding and conformational dynamicsEarly events in protein folding explored by rapid mixing methods.Ultrafast signals in protein folding and the polypeptide contracted state.Single-domain antibody fragments with high conformational stability.Limited internal friction in the rate-limiting step of a two-state protein folding reactionDiffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein foldingRapid refolding of a proline-rich all-beta-sheet fibronectin type III module
P2860
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P2860
Extremely rapid protein folding in the absence of intermediates.
description
1995 nî lūn-bûn
@nan
1995 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
name
Extremely rapid protein folding in the absence of intermediates.
@ast
Extremely rapid protein folding in the absence of intermediates.
@en
type
label
Extremely rapid protein folding in the absence of intermediates.
@ast
Extremely rapid protein folding in the absence of intermediates.
@en
prefLabel
Extremely rapid protein folding in the absence of intermediates.
@ast
Extremely rapid protein folding in the absence of intermediates.
@en
P2093
P2860
P356
P1476
Extremely rapid protein folding in the absence of intermediates.
@en
P2093
Marahiel MA
Schindler T
P2860
P304
P356
10.1038/NSB0895-663
P577
1995-08-01T00:00:00Z