Unravelling the folding of bacteriorhodopsin.
The folding mechanism of integral membrane proteins has eluded detailed study, largely as a result of the inherent difficulties in folding these proteins in vitro. The seven-transmembrane helical protein bacteriorhodopsin has, however, allowed major advances to be made, not just on the folding of this particular protein, but also on the factors governing folding of transmembrane alpha-helical proteins in general. This review focusses on kinetic and equilibrium studies of bacteriorhodopsin folding in vitro. It covers what is currently known about secondary and tertiary structure formation as well as the events accompanying retinal binding, for protein in detergent and lipid systems, including native membrane samples.
Booth
P J
PJ
Department of Biochemistry, Imperial College of Science, Technology and Medicine, South Kensington, SW7 2AZ, London, UK. paula.booth@bris.ac.uk
D001436:Bacteriorhodopsins / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry; D008563:Membrane Lipids / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D008051:Lipid Bilayers; D008563:Membrane Lipids; D001436:Bacteriorhodopsins