Identification of residual structure in the unfolded state of ribonuclease H1 from the moderately thermophilic Chlorobium tepidum: comparison with thermophilic and mesophilic homologues
about
Residual structure in unfolded proteinsThermal adaptation of conformational dynamics in ribonuclease HTake home lessons from studies of related proteinsStepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.The folding of single domain proteins--have we reached a consensus?Protein unfolding rates correlate as strongly as folding rates with native structure.Evidence of a folding intermediate in RNase H from single-molecule FRET experiments.The burst-phase folding intermediate of ribonuclease H changes conformation over evolutionary history.Under-folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis.
P2860
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P2860
Identification of residual structure in the unfolded state of ribonuclease H1 from the moderately thermophilic Chlorobium tepidum: comparison with thermophilic and mesophilic homologues
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Identification of residual str ...... ilic and mesophilic homologues
@ast
Identification of residual str ...... ilic and mesophilic homologues
@en
type
label
Identification of residual str ...... ilic and mesophilic homologues
@ast
Identification of residual str ...... ilic and mesophilic homologues
@en
prefLabel
Identification of residual str ...... ilic and mesophilic homologues
@ast
Identification of residual str ...... ilic and mesophilic homologues
@en
P2860
P356
P1433
P1476
Identification of residual str ...... ilic and mesophilic homologues
@en
P2093
Kathleen Ratcliff
Susan Marqusee
P2860
P304
P356
10.1021/BI1001097
P407
P577
2010-06-01T00:00:00Z