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Structure and Orientation of Ligands Bound to Membrane Proteins Are Reflected by Residual Dipolar Couplings in Solution NMR Measurements
Author(s) -
Koenig Bernd W.
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20021004)3:10<975::aid-cbic975>3.0.co;2-y
Subject(s) - transducin , rhodopsin , residual dipolar coupling , chemistry , nuclear magnetic resonance spectroscopy , crystallography , spins , ligand (biochemistry) , membrane , dipole , biophysics , stereochemistry , receptor , physics , biochemistry , biology , organic chemistry , retinal , condensed matter physics
Nuclear spins remember the past! The bound conformation of small ligands that are in fast exchange between a free and a membrane‐protein‐bound form can be obtained from solution NMR spectroscopy experiments on the free ligand (see figure). Transferred dipolar couplings characterize both the structure and orientation of a rhodopsin‐bound peptide that mimics a receptor binding region of the G protein transducin. A model for the mutual orientation of rhodopsin and transducin in the active complex is proposed.