Partial unfolding of diverse SH3 domains on a wide timescale.
about
SH3 domains come of ageHydrogen Exchange Mass Spectrometry of Related Proteins with Divergent Sequences: A Comparative Study of HIV-1 Nef Allelic Variants.Dynamics of the Tec-family tyrosine kinase SH3 domains.Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.Tyrosine phosphorylation in the SH3 domain disrupts negative regulatory interactions within the c-Abl kinase core.NMR evidence for forming highly populated helical conformations in the partially folded hNck2 SH3 domain.Abl N-terminal cap stabilization of SH3 domain dynamicsThe Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri TipInvestigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry.Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis.Hydrogen exchange mass spectrometry: what is it and what can it tell us?Dynamic protein ligand interactions--insights from MS.On the solution conformation and dynamics of the HIV-1 viral infectivity factorDynamic conformations of nucleophosmin (NPM1) at a key monomer-monomer interface affect oligomer stability and interactions with granzyme B.Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasomeAllosteric loss-of-function mutations in HIV-1 Nef from a long-term non-progressor.Structure and dynamic regulation of Abl kinases.Actin isoform-specific conformational differences observed with hydrogen/deuterium exchange and mass spectrometry.HDX-MS takes centre stage at unravelling kinase dynamics.Painting proteins with covalent labels: what's in the picture?Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities.Bottom-up hydrogen deuterium exchange mass spectrometry: data analysis and interpretation.Conformational analysis of processivity clamps in solution demonstrates that tertiary structure does not correlate with protein dynamics.Analyzing protein dynamics using hydrogen exchange mass spectrometry.Heat Shock Protein 90 kDa (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70.Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 2. Exchange kinetics.False EX1 signatures caused by sample carryover during HX MS analyses.The stress sigma factor of RNA polymerase RpoS/σS is a solvent exposed open molecule in solution.
P2860
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P2860
Partial unfolding of diverse SH3 domains on a wide timescale.
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Partial unfolding of diverse SH3 domains on a wide timescale.
@ast
Partial unfolding of diverse SH3 domains on a wide timescale.
@en
type
label
Partial unfolding of diverse SH3 domains on a wide timescale.
@ast
Partial unfolding of diverse SH3 domains on a wide timescale.
@en
prefLabel
Partial unfolding of diverse SH3 domains on a wide timescale.
@ast
Partial unfolding of diverse SH3 domains on a wide timescale.
@en
P1476
Partial unfolding of diverse SH3 domains on a wide timescale.
@en
P2093
Thomas E Wales
P304
P356
10.1016/J.JMB.2006.01.075
P407
P577
2006-02-06T00:00:00Z