Transmembrane protein topology mapping by the substituted cysteine accessibility method (SCAM™): Application to lipid-specific membrane protein topogenesis

Mikhail Bogdanov, Wei Zhang, Jun Xie, William Dowhan

Research output: Contribution to journalArticle

102 Scopus citations


We provide an overview of lipid-dependent polytopic membrane protein topogenesis, with particular emphasis on Escherichia coli strains genetically altered in their lipid composition and strategies for experimentally determining the transmembrane organization of proteins. A variety of reagents and experimental strategies are described including the use of lipid mutants and thiol-specific chemical reagents to study lipid-dependent and host-specific membrane protein topogenesis by substituted cysteine site-directed chemical labeling. Employing strains in which lipid composition can be controlled temporally during membrane protein synthesis and assembly provides a means to observe dynamic changes in protein topology as a function of membrane lipid composition.

Original languageEnglish (US)
Pages (from-to)148-171
Number of pages24
Issue number2 SPEC. ISS.
StatePublished - Jun 2005



  • Cysteine scanning
  • Maleimides
  • Membrane protein
  • Phosphatidylethanolamine
  • Phospholipid
  • Protein topology
  • Topogenesis

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this