The folding mechanisms of integral membrane proteins have largely eluded detailed study. This is owing to the inherent difficulties in folding these hydrophobic proteins in vitro, which, in turn, reflects the often apparently insurmountable problem of mimicking the natural membrane bilayer with lipid or detergent mixtures. There is, however, a large body of information on lipid properties and, in particular, on phosphatidylcholine and phosphatidylethanolamine lipids, which are common to many biological membranes. We have exploited this knowledge to develop efficient in vitro lipid-bilayer folding systems for the membrane protein, bacteriorhodopsin. Furthermore, we have shown that a rate-limiting apoprotein folding step and the overall folding efficiency appear to be controlled by particular properties of the lipid bilayer. The properties of interest are the stored curvature elastic energy within the bilayer, and the lateral pressure that the lipid chains exert on the their neighbouring folding proteins. These are generic properties of the bilayer that can be achieved with simple mixtures of biological lipids, and are not specific to the lipids studied here. These bilayer properties also seem to be important in modulating the function of several membrane proteins, as well as the function of membranes in vivo. Thus, it seems likely that careful manipulations of lipid properties will shed light on the forces that drive membrane protein folding, and will aid the development of bilayer folding systems for other membrane proteins.
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August 2001
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August 01 2001
Manipulating the folding of membrane proteins: using the bilayer to our advantage
Paula J. Booth;
Paula J. Booth
1
*Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, U.K.
1To whom correspondence should be addressed. Present address: Department of Biochemistry, University of Bristol, Bristol BS8 1TD, U.K.
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A. Rachael Curran;
A. Rachael Curran
2
*Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, U.K.
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Richard H. Templer;
Richard H. Templer
†Department of Chemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, U.K.
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Hui Lu;
Hui Lu
3
*Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, U.K.
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Wim Meijberg
Wim Meijberg
4
*Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, U.K.
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Publisher: Portland Press Ltd
Online ISSN: 1744-1439
Print ISSN: 0067-8694
© 2001 The Biochemical Society
2001
Biochem Soc Symp (2001) 68: 27–33.
Citation
Alan Berry, Sheena E. Radford, Paula J. Booth, A. Rachael Curran, Richard H. Templer, Hui Lu, Wim Meijberg; Manipulating the folding of membrane proteins: using the bilayer to our advantage. Biochem Soc Symp 1 August 2001; 68 27–33. doi: https://doi.org/10.1042/bss0680027
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