title: 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.
authors.affiliation: Institute of Structural and Molecular Biology, Birkbeck College, University of London, Malet Street, London, WC1E 7HX, UK. b.wallace@mail.cryst.bbk.ac.uk.
authors.forename: A J
authors.initials: AJ
authors.lastname: Miles
authors.forename: B A
authors.initials: BA
authors.lastname: Wallace
mesh_terms: D002942:Circular Dichroism; D008055:Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D055550:Protein Stability; D058767:Protein Unfolding; D012995:Solubility; D012997:Solvents / Q000737:chemistry; D017356:Synchrotrons
chemical_list: D008055:Lipids; D008565:Membrane Proteins; D012997:Solvents