Kinetic traps in the folding of beta alpha-repeat proteins: CheY initially misfolds before accessing the native conformation.
about
Environment-dependent long-range structural distortion in a temperature-sensitive point mutantClusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stability.Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo.Modulation of frustration in folding by sequence permutation.Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β parallel protein.Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental study.Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.Insights from coarse-grained Gō models for protein folding and dynamics.Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate stateAtomistic structural ensemble refinement reveals non-native structure stabilizes a sub-millisecond folding intermediate of CheY.Folding of proteins with a flavodoxin-like architecture.Non-native hydrophobic interactions detected in unfolded apoflavodoxin by paramagnetic relaxation enhancement.Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins.Non-native structure appears in microseconds during the folding of E. coli RNase H.Interrupted hydrogen/deuterium exchange reveals the stable core of the remarkably helical molten globule of alpha-beta parallel protein flavodoxin.Subdomain competition, cooperativity, and topological frustration in the folding of CheY.Structural Rearrangement upon Fragmentation of the Stability Core of the ALS-Linked Protein TDP-43.
P2860
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P2860
Kinetic traps in the folding of beta alpha-repeat proteins: CheY initially misfolds before accessing the native conformation.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
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2008年學術文章
@zh-hant
name
Kinetic traps in the folding o ...... ssing the native conformation.
@en
Kinetic traps in the folding o ...... ssing the native conformation.
@nl
type
label
Kinetic traps in the folding o ...... ssing the native conformation.
@en
Kinetic traps in the folding o ...... ssing the native conformation.
@nl
prefLabel
Kinetic traps in the folding o ...... ssing the native conformation.
@en
Kinetic traps in the folding o ...... ssing the native conformation.
@nl
P2093
P1476
Kinetic traps in the folding o ...... ssing the native conformation.
@en
P2093
C Robert Matthews
Louise A Wallace
Sagar V Kathuria
P304
P356
10.1016/J.JMB.2008.06.054
P407
P50
P577
2008-06-28T00:00:00Z