PMID: 9427005Jan 1, 1997Paper

Folding alpha-helical membrane proteins: kinetic studies on bacteriorhodopsin

Folding & Design
Paula J Booth

Abstract

The correct folding and assembly of proteins within biological membranes is essential for membrane biogenesis and function. In contrast to the large body of work on water-soluble protein folding, however, very little is known about how membrane proteins fold to their final structures. Recent biophysical studies on membrane-protein folding in vitro are beginning to shed light on this problem. In particular, the forces that the membrane lipids impose on the folding protein appear to control certain events. The seven-helix transmembrane protein bacteriorhodopsin has been the focus of much attention and kinetic studies on the folding of this protein form the basis of this review.

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Citations

Dec 16, 2003·Journal of Molecular Biology·Mar OrzáezIsmael Mingarro
Jan 17, 2012·Biochemistry·Venkatramanan KrishnamaniJanos K Lanyi
Jul 17, 1998·Nature Structural Biology·C M Dobson, P J Hore
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Nov 5, 2014·Journal of the American Chemical Society·Jonathan P SchlebachChiwook Park
Sep 8, 2004·Journal of Molecular Biology·Samantha J AllenPaula J Booth
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Sep 14, 2000·Biochimica Et Biophysica Acta·P J Booth
Jul 25, 2014·Archives of Biochemistry and Biophysics·Jennifer NeumannDirk Schneider
Dec 3, 2004·Biophysical Journal·Harald JanovjakAndrew D L Humphris
Jan 24, 2006·Journal of Molecular Biology·Emma L R ComptonPaula J Booth
May 11, 2006·Chemical Reviews·Kevin R Mackenzie

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