title: 1H-NMR study of endothelin, sequence-specific assignment of the spectrum and a solution structure.
abstract: The solution conformation of the recently discovered bi-cyclic, 21 amino acid vasoconstrictor peptide, Endothelin I, has been examined by 1H-NMR in deuterated dimethyl sulphoxide. A full sequential assignment has been achieved. In addition, 19 long range NOEs were detected which were employed as distance constraints in molecular dynamics calculations to yield a possible solution structure for this new peptide.
authors.affiliation: Merrell Dow Research Institute, Strasbourg, France.
authors.forename: V
authors.initials: V
authors.lastname: Saudek
authors.forename: J
authors.initials: J
authors.lastname: Hoflack
authors.forename: J T
authors.initials: JT
authors.lastname: Pelton
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016232:Endothelins; D004730:Endothelium, Vascular; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides; D011487:Protein Conformation; D012984:Software; D012996:Solutions
chemical_list: D016232:Endothelins; D010455:Peptides; D012996:Solutions; D006859:Hydrogen