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Biophys. J. BioFAST: First Published January 11, 2008. doi:10.1529/biophysj.107.121848
© 2008 by the Biophysical Society.


A more recent version of this article appeared on May 1, 2008.
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Yann Gohon
Tassadite Dahmane
Rob W. H. Ruigrok
Peter Schuck
Fabrice Rappaport
Peter Timmins
Donald M. Engelman
Christophe Tribet
Jean-Luc Popot
Christine Ebel
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MEMBRANES

Bacteriorhodopsin/amphipol complexes: structural and functional properties

Yann Gohon 1, Tassadite Dahmane 2, Rob W. H. Ruigrok 3, Peter Schuck 4, Delphine Charvolin 2, Fabrice Rappaport 5, Peter Timmins 6, Donald M. Engelman 7, Christophe Tribet 8, Jean-Luc Popot 2 and Christine Ebel 9*

1 Inra
2 IBPC, CNRS and Université Paris-7, France.
3 Unit for Virus Host Cell Interactions, UJF-EMBL-CNRS France.
4 National Institutes of Health
5 Institut de Biologie Physico-Chimique
6 Large Scale Structures Group, Institut Laue-Langevin, France
7 Molecular Biophysics and Biochemistry, Yale University, USA.
8 PPMD, CNRS-ESPCI, France.
9 Institut de Biologie Structurale, CNRS, CEA, Université Joseph Fourier

* To whom correspondence should be addressed. E-mail: christine.ebel{at}ibs.fr.

Submitted on September 11, 2007
Revised on October 18, 2007
Accepted on 14 December 2007


   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. Following 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, ~2 g of APol per g of BR, arranged in a compact layer. In the absence of free APol, BR/APol particles can auto-associate into small or large ordered fibrils.

Key Words: amphipathic polymers, analytical ultracentrifugation, electron microscopy, membrane proteins, small angle neutron scattering, surfactants







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Copyright © 2008 by the Biophysical Society.