SPECTRAL METHODS FOR STUDY OF THE G-PROTEIN-COUPLED RECEPTOR RHODOPSIN. I. VIBRATIONAL AND ELECTRONIC SPECTROSCOPY

Overview

Journal Opt Spectrosc

Date 2017 Mar 7

PMID 28260815

Citations 2

Authors

A V Struts

A V Barmasov

M F Brown

Affiliations

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Abstract

Here we review the application of modern spectral methods for the study of G-protein-coupled receptors (GPCRs) using rhodopsin as a prototype. Because X-ray analysis gives us immobile snapshots of protein conformations, it is imperative to apply spectroscopic methods for elucidating their function: vibrational (Raman, FTIR), electronic (UV-visible absorption, fluorescence) spectroscopies, and magnetic resonance (electron paramagnetic resonance, EPR), and nuclear magnetic resonance, NMR). In the first of the two companion articles, we discuss the application of optical spectroscopy for studying rhodopsin in a membrane environment. Information is obtained regarding the time-ordered sequence of events in rhodopsin activation. Isomerization of the chromophore and deprotonation of the retinal Schiff base leads to a structural change of the protein involving the motion of helices H5 and H6 in a pH-dependent process. Information is obtained that is unavailable from X-ray crystallography, which can be combined with spectroscopic studies to achieve a more complete understanding of GPCR function.

Citing Articles

Nicotinamide phosphoribosyltransferase purification using SUMO expression system.

Molugu T, Oita R, Chawla U, Camp S, Brown M, Garcia J Anal Biochem. 2020; 598:113597.

PMID: 31982408 PMC: 7735423. DOI: 10.1016/j.ab.2020.113597.

CONDENSED-MATTER SPECTROSCOPY SPECTRAL METHODS FOR STUDY OF THE G-PROTEIN-COUPLED RECEPTOR RHODOPSIN. II. MAGNETIC RESONANCE METHODS.

Struts A, Barmasov A, Brown M Opt Spectrosc. 2017; 120(2):286-293.

PMID: 28260816 PMC: 5334789. DOI: 10.1134/S0030400X16010197.

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