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A functional NMR for membrane proteins: dynamics, ligand binding, and allosteric modulation
Author(s) -
Oxenoid Kirill,
Chou James J.
Publication year - 2016
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2910
Subject(s) - allosteric regulation , chemistry , biophysics , allosteric enzyme , conformational change , ligand (biochemistry) , protein dynamics , membrane protein , membrane , molecular dynamics , stereochemistry , biochemistry , computational chemistry , receptor , biology
Abstract By nature of conducting ions, transporting substrates and transducing signals, membrane channels, transporters and receptors are expected to exhibit intrinsic conformational dynamics. It is therefore of great interest and importance to understand the various properties of conformational dynamics acquired by these proteins, for example, the relative population of states, exchange rate, conformations of multiple states, and how small molecule ligands modulate the conformational exchange. Because small molecule binding to membrane proteins can be weak and/or dynamic, structural characterization of these effects is very challenging. This review describes several NMR studies of membrane protein dynamics, ligand‐induced conformational rearrangements, and the effect of ligand binding on the equilibrium of conformational exchange. The functional significance of the observed phenomena is discussed.