Bacteriorhodopsin/amphipol complexes: Structural and functional properties

被引:79
作者
Gohon, Yann [3 ,4 ]
Dahmane, Tassadite [3 ,4 ]
Ruigrok, Rob W. H. [5 ]
Schuck, Peter
Charvolin, Delphine
Rappaport, Fabrice [7 ,8 ]
Timmins, Peter [9 ]
Engelman, Donald M. [10 ]
Tribet, Christophe [11 ]
Popot, Jean-Luc [3 ,4 ]
Ebel, Christine [1 ,2 ,6 ]
机构
[1] Univ Grenoble 1, F-38027 Grenoble, France
[2] IBS, CNRS, Mol Biophys Lab, CEA,DSV, F-38027 Grenoble, France
[3] Univ Paris 07, Inst Biol Phys Chim, F-75005 Paris, France
[4] CNRS, Lab Phys Chim Mol Membranes Biol, F-75005 Paris, France
[5] Unit Virus Host Cell Interact, Grenoble, France
[6] NIH, PBR, DBPS, ORS, Bethesda, MD USA
[7] CNRS, Paris, France
[8] Univ Paris 06, Inst Biol Phys Chim, Paris, France
[9] Inst Max Von Laue Paul Langevin, Large Scale Struct Grp, Grenoble, France
[10] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT USA
[11] CNRS, Lab Phys Chim Polymeres & Milieux Disperses, Paris, France
关键词
D O I
10.1529/biophysj.107.121848
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
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. ash, 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, similar to 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.
引用
收藏
页码:3523 / 3537
页数:15
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