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Cell Mol Life Sci. 2010 Jun;67(11):1779-98. doi: 10.1007/s00018-010-0259-0. Epub 2010 Jan 27.

Protein folding in membranes.

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  • 1Leibniz Institute of Molecular Pharmacology (FMP), Robert-Rössle-Str. 10, 13125, Berlin, Germany.

Abstract

Separation of cells and organelles by bilayer membranes is a fundamental principle of life. Cellular membranes contain a baffling variety of proteins, which fulfil vital functions as receptors and signal transducers, channels and transporters, motors and anchors. The vast majority of membrane-bound proteins contain bundles of alpha-helical transmembrane domains. Understanding how these proteins adopt their native, biologically active structures in the complex milieu of a membrane is therefore a major challenge in today's life sciences. Here, we review recent progress in the folding, unfolding and refolding of alpha-helical membrane proteins and compare the molecular interactions that stabilise proteins in lipid bilayers. We also provide a critical discussion of a detergent denaturation assay that is increasingly used to determine membrane-protein stability but is not devoid of conceptual difficulties.

PMID:
20101433
[PubMed - indexed for MEDLINE]
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