title: SARS coronavirus E protein in phospholipid bilayers: an x-ray study.
abstract: We investigated the structure of the hydrophobic domain of the severe acute respiratory syndrome E protein in model lipid membranes by x-ray reflectivity and x-ray scattering. In particular, we used x-ray reflectivity to study the location of an iodine-labeled residue within the lipid bilayer. The label imposes spatial constraints on the protein topology. Experimental data taken as a function of protein/lipid ratio P/L and different swelling states support the hairpin conformation of severe acute respiratory syndrome E protein reported previously. Changes in the bilayer thickness and acyl-chain ordering are presented as a function of P/L, and discussed in view of different structural models.
authors.affiliation: Institute for X-ray Physics, University of Göttingen, Göttingen, Germany.
authors.forename: Z
authors.initials: Z
authors.lastname: Khattari
authors.forename: G
authors.initials: G
authors.lastname: Brotons
authors.forename: M
authors.initials: M
authors.lastname: Akkawi
authors.forename: E
authors.initials: E
authors.lastname: Arbely
authors.forename: I T
authors.initials: IT
authors.lastname: Arkin
authors.forename: T
authors.initials: T
authors.lastname: Salditt
mesh_terms: D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008560:Membrane Fluidity; D008565:Membrane Proteins / Q000737:chemistry / Q000648:ultrastructure; D044367:Phase Transition; D010743:Phospholipids / Q000737:chemistry*; D011487:Protein Conformation; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D000086082:Viroporin Proteins; D014961:X-Ray Diffraction
chemical_list: C501689:E protein, SARS coronavirus; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010743:Phospholipids; D014759:Viral Envelope Proteins; D000086082:Viroporin Proteins; D004134:Dimyristoylphosphatidylcholine