Issue 18, 2016

Circular dichroism spectroscopy of membrane proteins

Abstract

Circular dichroism (CD) spectroscopy is a well-established technique for studying the secondary structures, dynamics, folding pathways, and interactions of soluble proteins, and is complementary to the high resolution but generally static structures produced by X-ray crystallography, NMR spectroscopy, and cryo electron microscopy. CD spectroscopy has special relevance for the study of membrane proteins, which are difficult to crystallise and largely ignored in structural genomics projects. However, the requirement for membrane proteins to be embedded in amphipathic environments such as membranes, lipid vesicles, detergent micelles, bicelles, oriented bilayers, or nanodiscs, in order for them to be soluble or dispersed in solution whilst maintaining their structure and function, necessitates the use of different experimental and analytical approaches than those employed for soluble proteins. This review discusses specialised methods for collecting and analysing membrane protein CD data, highlighting where protocols for soluble and membrane proteins diverge.

Graphical abstract: Circular dichroism spectroscopy of membrane proteins

Article information

Article type
Tutorial Review
Submitted
29 1月 2015
First published
27 6月 2016
This article is Open Access
Creative Commons BY-NC license

Chem. Soc. Rev., 2016,45, 4859-4872

Circular dichroism spectroscopy of membrane proteins

A. J. Miles and B. A. Wallace, Chem. Soc. Rev., 2016, 45, 4859 DOI: 10.1039/C5CS00084J

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