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Issue 18, 2016
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Circular dichroism spectroscopy of membrane proteins

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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

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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
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    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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