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Magic angle spinning nuclear magnetic resonance spectroscopy of G protein-coupled receptors

Goncalves, J and Eilers, M and South, K and Opefi, CA and Laissue, PP and Reeves, PJ and Smith, SO (2013) 'Magic angle spinning nuclear magnetic resonance spectroscopy of G protein-coupled receptors.' In: Conn, P Michael, (ed.) G Protein Coupled Receptors Modeling, Activation, Interactions and Virtual Screening. Methods in Enzymology, 522 . Elsevier, 365 - 389. ISBN 9780124078659

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Abstract

G protein-coupled receptors (GPCRs) represent the largest family of membrane receptors and mediate a diversity of cellular processes. These receptors have a common seven-transmembrane helix structure, yet have evolved to respond to literally thousands of different ligands. In this chapter, we describe the use of magic angle spinning solid-state NMR spectroscopy for characterizing the structure and dynamics of GPCRs. Solid-state NMR spectroscopy is well suited for structural measurements in both detergent micelles and membrane bilayer environments. We first outline the methods for large-scale production of stable, functional receptors containing 13 C- and 15 N-labeled amino acids. The expression methods make use of eukaryotic HEK293S cell lines that produce correctly folded, fully functional receptors. We subsequently describe the basic methods used for magic angle spinning solid-state NMR measurements of chemical shifts and dipolar couplings, which reveal detailed information on GPCR structure and dynamics. © 2013 Elsevier Inc.

Item Type: Book Section
Uncontrolled Keywords: GPCR; Solid-state NMR; Rhodopsin; Expression; HEK293; Membrane proteins
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Users 161 not found.
Date Deposited: 07 Jan 2015 15:03
Last Modified: 14 Oct 2019 18:18
URI: http://repository.essex.ac.uk/id/eprint/10407

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