Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs

Timothy H. Bayburt, Yelena V. Grinkova, Stephen G. Sligar

Research output: Contribution to journalArticlepeer-review


Nanodiscs, phospholipid bilayer assemblies of controlled size, were used to self-assemble bacteriorhodopsin (bR) into single trimers. Self-assembly at optimal bR to Nanodisc and phospholipid stoichiometry yielded particles containing three bR molecules. Analysis of solution small angle X-ray scattering indicated that bacteriorhodopsin is embedded in a discoidal phospholipid bilayer structure. Formation of trimers, as evidenced by visible circular dichroism of the retinal absorbance bands, is facilitated in Nanodiscs at a specific size threshold, suggesting that a critical bilayer area or amount of lipid is necessary to maintain a native oligomeric state. The lipid to bR ratio in the assembly process was also found to be an important factor in determining oligomerization state. These nanoscale bilayers offer the opportunity to understand and control the assembly of oligomeric integral membrane proteins critical to macromolecular recognition and cellular signaling.

Original languageEnglish (US)
Pages (from-to)215-222
Number of pages8
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - Jun 15 2006


  • Bicelle
  • Membrane protein
  • Model bilayer
  • Nanoparticle
  • Oligomer
  • Self-assembly

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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