Jump to main content
Jump to site search

Issue 18, 2016
Previous Article Next Article

Circular dichroism spectroscopy of membrane proteins

Author affiliations

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

Back to tab navigation
Please wait while Download options loads

Publication details

The article was received on 29 Jan 2015 and first published on 27 Jun 2016


Article type: Tutorial Review
DOI: 10.1039/C5CS00084J
Citation: Chem. Soc. Rev., 2016,45, 4859-4872
  • Open access: Creative Commons BY-NC license
  •   Request permissions

    Circular dichroism spectroscopy of membrane proteins

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

Search articles by author