Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers

Timothy H. Bayburt, Stephen G. Sligar

Research output: Contribution to journalArticlepeer-review


One of the biggest challenges in pharmaceutical research is obtaining integral membrane proteins in a functional, solubilized, and monodisperse state that provides a native-like environment that maintains the spectrum of in vivo activities. Many of these integral membrane proteins are receptors, enzymes, or other macromolecular assemblies that are important drug targets. An example is the general class of proteins composed of seven-transmembrane segments (7-TM) as exemplified by the G-protein-coupled receptors. In this article, we describe a simple system for self-assembling bacteriorhodopsin, as a model protein containing 7-TM helices, with phospholipids to form a nanometer-scale soluble bilayer structure encircled by a 200 amino acid scaffold protein. The result is the single molecule incorporation of an integral membrane protein target into a soluble and monodisperse structure that allows the structural and functional tools of solution biochemistry to be applied.

Original languageEnglish (US)
Pages (from-to)2476-2481
Number of pages6
JournalProtein Science
Issue number11
StatePublished - Nov 2003


  • Bilayer
  • Membrane proteomics
  • Nanodisc
  • Phospholipid
  • Self-assembly
  • Seven-transmembrane protein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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