title: High resolution 1H NMR study of the solution structure of the S4 segment of the sodium channel protein.
abstract: A peptide (S4) of the rat brain sodium channel has been synthesized, studied by high-resolution NMR and its secondary structure modelled by distance geometry and restrained molecular dynamics techniques.
authors.affiliation: Department of Biochemistry, University of Oxford, England.
authors.forename: D
authors.initials: D
authors.lastname: Mulvey
authors.forename: G F
authors.initials: GF
authors.lastname: King
authors.forename: R M
authors.initials: RM
authors.lastname: Cooke
authors.forename: D G
authors.initials: DG
authors.lastname: Doak
authors.forename: T S
authors.initials: TS
authors.lastname: Harvey
authors.forename: I D
authors.initials: ID
authors.lastname: Campbell
mesh_terms: D000595:Amino Acid Sequence; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008565:Membrane Proteins / Q000302:isolation & purification; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis; D011487:Protein Conformation; D015222:Sodium Channels / Q000032:analysis*
chemical_list: D008565:Membrane Proteins; D010446:Peptide Fragments; D015222:Sodium Channels; D006859:Hydrogen