Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange.
about
Local conformational dynamics in alpha-helices measured by fast triplet transferThe Unfolding MD Simulations of Cyclophilin: Analyzed by Surface Contact Networks and Their Associated MetricsMechanisms and uses of hydrogen exchange.Future directions in folding: the multi-state nature of protein structure.Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques.Proteolytic degradation of ribonuclease A in the pretransition region of thermally and urea-induced unfolding.An unlocking/relocking barrier in conformational fluctuations of villin headpiece subdomainStopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase.Cytochrome c folding pathway: kinetic native-state hydrogen exchange.Limited proteolysis of ribonuclease A with thermolysin in trifluoroethanol.Proteins unfold in stepsInterplay between drying and stability of a TIM barrel protein: a combined simulation-experimental study.The folding pathway of T4 lysozyme: an on-pathway hidden folding intermediateClusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.Direct evidence for a dry molten globule intermediate during the unfolding of a small protein.A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions.Stability and folding of amphibian ribonuclease A superfamily members in comparison with mammalian homologues.Dry molten globule intermediates and the mechanism of protein unfolding.Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR.A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding.Determinants of protein hydrogen exchange studied in equine cytochrome c.Trifluoroethanol-induced conformational transitions of proteins: insights gained from the differences between alpha-lactalbumin and ribonuclease A.Hydrogen-bond disruption probability in proteins by a modified self-consistent harmonic approach.Pathway heterogeneity in protein folding
P2860
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P2860
Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange.
description
1995 nî lūn-bûn
@nan
1995 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մարտին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Kinetics of hydrogen bond brea ...... d by pulsed hydrogen exchange.
@ast
Kinetics of hydrogen bond brea ...... d by pulsed hydrogen exchange.
@en
Kinetics of hydrogen bond brea ...... d by pulsed hydrogen exchange.
@nl
type
label
Kinetics of hydrogen bond brea ...... d by pulsed hydrogen exchange.
@ast
Kinetics of hydrogen bond brea ...... d by pulsed hydrogen exchange.
@en
Kinetics of hydrogen bond brea ...... d by pulsed hydrogen exchange.
@nl
prefLabel
Kinetics of hydrogen bond brea ...... d by pulsed hydrogen exchange.
@ast
Kinetics of hydrogen bond brea ...... d by pulsed hydrogen exchange.
@en
Kinetics of hydrogen bond brea ...... d by pulsed hydrogen exchange.
@nl
P2860
P356
P1476
Kinetics of hydrogen bond brea ...... d by pulsed hydrogen exchange.
@en
P2093
R L Baldwin
T Kiefhaber
P2860
P304
P356
10.1073/PNAS.92.7.2657
P407
P577
1995-03-01T00:00:00Z