Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip
about
Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.The Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein.Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 2. Exchange kinetics.
P2860
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
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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
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name
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip
@ast
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip
@en
type
label
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip
@ast
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip
@en
prefLabel
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip
@ast
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip
@en
P2860
P356
P1433
P1476
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip
@en
P2093
Bartholomew M Sefton
Peter Kjellen
P2860
P304
P356
10.1110/PS.052016406
P577
2006-10-01T00:00:00Z