title: Structure characterization of membrane bound and surface adsorbed protein.
abstract: X-ray standing waves (XSW) have been used to study the topology of the protein cytochrome c, bound to a negatively charged model membrane and adsorbed at a metal surface. At the metal surface, cytochrome c forms an hexagonally close-packed monolayer. A similar packing arrangement is observed at the surface of a self-assembled lipid film on silver. The data suggest that cytochrome c maintains its native globular structure upon surface binding and subsequent storage for an extended period. Further, the data are consistent with a protein docking mechanism wherein the heme plane is oriented perpendicular to and with its exposed edge facing the surface. This study demonstrates the utility of XSW as a new and powerful structural tool for investigating membrane- and surface-protein interactions.
authors.affiliation: Department of Chemistry, Ohio State University, Columbus 43210.
authors.forename: J
authors.initials: J
authors.lastname: Wang
authors.forename: C J
authors.initials: CJ
authors.lastname: Wallace
authors.forename: I
authors.initials: I
authors.lastname: Clark-Lewis
authors.forename: M
authors.initials: M
authors.lastname: Caffrey
mesh_terms: D000327:Adsorption; D003574:Cytochrome c Group / Q000737:chemistry; D005453:Fluorescence; D008565:Membrane Proteins / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D012645:Selenomethionine; D012834:Silver; D014965:X-Rays
chemical_list: D003574:Cytochrome c Group; D008565:Membrane Proteins; D011506:Proteins; D012834:Silver; D012645:Selenomethionine