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Biochim Biophys Acta. 2011 Aug;1808(8):1957-74. doi: 10.1016/j.bbamem.2011.03.016. Epub 2011 Apr 6.

Choosing membrane mimetics for NMR structural studies of transmembrane proteins.

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1
Department of Chemistry, Pharmaqam/NanoQAM, Université du Québec à Montréal, Downtown Station, Montréal, Canada H3C 3P8. Dror.Warschawski@ibpc.fr

Abstract

The native environment of membrane proteins is complex and scientists have felt the need to simplify it to reduce the number of varying parameters. However, experimental problems can also arise from oversimplification which contributes to why membrane proteins are under-represented in the protein structure databank and why they were difficult to study by nuclear magnetic resonance (NMR) spectroscopy. Technological progress now allows dealing with more complex models and, in the context of NMR studies, an incredibly large number of membrane mimetics options are available. This review provides a guide to the selection of the appropriate model membrane system for membrane protein study by NMR, depending on the protein and on the type of information that is looked for. Beside bilayers (of various shapes, sizes and lamellarity), bicelles (aligned or isotropic) and detergent micelles, this review will also describe the most recent membrane mimetics such as amphipols, nanodiscs and reverse micelles. Solution and solid-state NMR will be covered as well as more exotic techniques such as DNP and MAOSS.

PMID:
21477581
DOI:
10.1016/j.bbamem.2011.03.016
[Indexed for MEDLINE]
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