Spectral methods for study of the G-protein-coupled receptor rhodopsin. II. Magnetic resonance methods

A. V. Struts, A. V. Barmasov, Michael F Brown

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

This article continues our review of spectroscopic studies of G-protein-coupled receptors. Magnetic resonance methods including electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) provide specific structural and dynamical data for the protein in conjunction with optical methods (vibrational, electronic spectroscopy) as discussed in the accompanying article. An additional advantage is the opportunity to explore the receptor proteins in the natural membrane lipid environment. Solid-state 2H and 13C NMR methods yield information about both the local structure and dynamics of the cofactor bound to the protein and its light-induced changes. Complementary site-directed spin-labeling studies monitor the structural alterations over larger distances and correspondingly longer time scales. A multiscale reaction mechanism describes how local changes of the retinal cofactor unlock the receptor to initiate large-scale conformational changes of rhodopsin. Activation of the G-protein-coupled receptor involves an ensemble of conformational substates within the rhodopsin manifold that characterize the dynamically active receptor.

Original languageEnglish (US)
Pages (from-to)286-293
Number of pages8
JournalOptics and Spectroscopy (English translation of Optika i Spektroskopiya)
Volume120
Issue number2
DOIs
StatePublished - Feb 1 2016

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Atomic and Molecular Physics, and Optics

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