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A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues
Author(s) -
Long Dong,
Marshall Christopher B.,
Bouvignies Guillaume,
MazhabJafari Mohammad T.,
Smith Matthew J.,
Ikura Mitsuhiko,
Kay Lewis E.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201305434
Subject(s) - gtp' , gtpase , chemistry , rheb , conformational isomerism , nuclear magnetic resonance spectroscopy , computer science , biophysics , computational biology , stereochemistry , biochemistry , biology , organic chemistry , phosphorylation , molecule , protein kinase b , mtorc1 , enzyme
Conformational Exchange : Small GTPases, such as Ras and Rheb, exchange between major and minor conformers when bound to GTP, with different functional properties for each state (see picture). Two‐dimensional 15 N CEST NMR spectroscopy is used to quantify the exchange parameters for both Ras and Rheb complexed with physiological GTP and the analogues GTPγS and GppNHp.