Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods.
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Cavities determine the pressure unfolding of proteinsNonuniform chain collapse during early stages of staphylococcal nuclease folding detected by fluorescence resonance energy transfer and ultrarapid mixing methodsComparison of Two ESI MS Based H/D Exchange Methods for Extracting Protein Folding Energies.Probing the folding intermediate of Bacillus subtilis RNase P protein by nuclear magnetic resonance.Nonlocal interactions are responsible for tertiary structure formation in staphylococcal nuclease.The role of the local environment of engineered Tyr to Trp substitutions for probing the denaturation mechanism of FIS.Experimental evolution of a green fluorescent protein composed of 19 unique amino acids without tryptophan.
P2860
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P2860
Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods.
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին 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
Folding kinetics of staphyloco ...... ring and rapid mixing methods.
@ast
Folding kinetics of staphyloco ...... ring and rapid mixing methods.
@en
type
label
Folding kinetics of staphyloco ...... ring and rapid mixing methods.
@ast
Folding kinetics of staphyloco ...... ring and rapid mixing methods.
@en
prefLabel
Folding kinetics of staphyloco ...... ring and rapid mixing methods.
@ast
Folding kinetics of staphyloco ...... ring and rapid mixing methods.
@en
P2093
P2860
P1476
Folding kinetics of staphyloco ...... ring and rapid mixing methods.
@en
P2093
Dimitry A Dolgikh
Heinrich Roder
Hong Cheng
Kosuke Maki
P2860
P304
P356
10.1016/J.JMB.2007.02.006
P407
P577
2007-02-09T00:00:00Z