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Biophys J. 2008 May 1;94(9):3523-37. doi: 10.1529/biophysj.107.121848. Epub 2008 Jan 11.

Bacteriorhodopsin/amphipol complexes: structural and functional properties.

Author information

1
Laboratoire de Physico-Chimie Moléculaire des Membranes Biologiques, Centre National de la Recherche Scientifique, and Université Paris-7, Institut de Biologie Physico-Chimique, Paris, France.

Abstract

The membrane protein bacteriorhodopsin (BR) can be kept soluble in its native state for months in the absence of detergent by amphipol (APol) A8-35, an amphiphilic polymer. After an actinic flash, A8-35-complexed BR undergoes a complete photocycle, with kinetics intermediate between that in detergent solution and that in its native membrane. BR/APol complexes form well defined, globular particles comprising a monomer of BR, a complete set of purple membrane lipids, and, in a peripheral distribution, approximately 2 g APol/g BR, arranged in a compact layer. In the absence of free APol, BR/APol particles can autoassociate into small or large ordered fibrils.

PMID:
18192360
PMCID:
PMC2292372
DOI:
10.1529/biophysj.107.121848
[Indexed for MEDLINE]
Free PMC Article

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