title: Mapping lipid and detergent molecules at the surface of membrane proteins.
abstract: Electron-density maps for the crystal structures of membrane proteins often show features suggesting binding of lipids and/or detergent molecules on the hydrophobic surface, but usually it is difficult to identify the bound molecules. In our studies, heavy-atom-labelled phospholipids and detergents have been used to unequivocally identify these binding sites at the surfaces of test membrane proteins, the reaction centres from Rhodobacter sphaeroides and Blastochloris viridis. The generality of this method is discussed in the present article.
authors: Institute of Molecular Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, Glasgow Biomedical Research Centre, University Place, Glasgow, U.K. r.cogdell@bio.gla.ac.uk
authors: Richard J
authors: RJ
authors: Cogdell
authors: Alastair T
authors: AT
authors: Gardiner
authors: Aleksander W
authors: AW
authors: Roszak
authors: Sigitas
authors: S
authors: Stončius
authors: Pavel
authors: P
authors: Kočovský
authors: Neil W
authors: NW
authors: Isaacs