Bacteriorhodopsin/amphipol Complexes: Structural and Functional Properties

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 2008 Jan 15

PMID 18192360

Citations 52

Authors

Yann Gohon

Tassadite Dahmane

Rob W H Ruigrok

Peter Schuck

Delphine Charvolin

Fabrice Rappaport

Peter Timmins

Donald M Engelman

Christophe Tribet

Jean-Luc Popot

Christine Ebel

Affiliations

Soon will be listed here.

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.

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