Heteronuclear NMR studies of the combined Src homology domains 2 and 3 of pp60 c-Src: effects of phosphopeptide binding
about
Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.Mobility of TOAC spin-labelled peptides binding to the Src SH3 domain studied by paramagnetic NMRDynamically Coupled Residues within the SH2 Domain of FYN Are Key to Unlocking Its ActivityAn examination of dynamics crosstalk between SH2 and SH3 domains by hydrogen/deuterium exchange and mass spectrometry.
P2860
Heteronuclear NMR studies of the combined Src homology domains 2 and 3 of pp60 c-Src: effects of phosphopeptide binding
description
im November 1997 veröffentlicher wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в листопаді 1997
@uk
name
Heteronuclear NMR studies of t ...... ects of phosphopeptide binding
@en
Heteronuclear NMR studies of t ...... ects of phosphopeptide binding
@nl
type
label
Heteronuclear NMR studies of t ...... ects of phosphopeptide binding
@en
Heteronuclear NMR studies of t ...... ects of phosphopeptide binding
@nl
prefLabel
Heteronuclear NMR studies of t ...... ects of phosphopeptide binding
@en
Heteronuclear NMR studies of t ...... ects of phosphopeptide binding
@nl
P2093
P1433
P1476
Heteronuclear NMR studies of t ...... ects of phosphopeptide binding
@en
P2093
D I Shalloway
G W Vuister
L K Nicholson
L N Gentile
S J Taylor
P304
P407
P577
1997-11-25T00:00:00Z