Bacteriorhodopsin/amphipol complexes: structural and functional properties.

نویسندگان

  • 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
چکیده

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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عنوان ژورنال:
  • Biophysical journal

دوره 94 9  شماره 

صفحات  -

تاریخ انتشار 2008