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J Mol Biol. 2004 Sep 24;342(4):1293-304.

Controlling the folding efficiency of an integral membrane protein.

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Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, UK.


Research into the folding mechanisms of integral membrane proteins lags far behind that of water-soluble proteins, to the extent that the term protein folding is synonymous with water-soluble proteins. Hydrophobic membrane proteins, and particularly those with transmembrane alpha-helical motifs, are frequently considered too difficult to work with. We show that the stored curvature elastic stress of lipid bilayers can be used to guide the design of efficient folding systems for these integral membrane proteins. The curvature elastic stress of synthetic phosphatidylcholine/phosphatidylethanolamine lipid bilayers can be used to control both the rate of folding and the yield of folded protein. The use of a physical bilayer property generalises this approach beyond the particular chemistry of the lipids involved.

[Indexed for MEDLINE]

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