title: Conformation of a cyclic opioid peptide analog by NMR and molecular dynamics simulation.
abstract: The conformation of a new Ty-c[Lys-Phe-Asp]-NH2 cyclic opioid peptide synthesized by solid phase method, has been determined from two-dimensional NMR and distance geometry followed by restrained molecular dynamics simulation. The conformation of the ring is well-defined, but the exocylic Tyr-1 and Phe-3 side-chain moiety possesses significant orientational freedom.
authors.affiliation: Chemistry Department, National Tsing Hua University, Hsinchu, Taiwan.
authors.forename: L C
authors.initials: LC
authors.lastname: Chuang
authors.forename: S T
authors.initials: ST
authors.lastname: Chen
authors.forename: C
authors.initials: C
authors.lastname: Ya
mesh_terms: D000595:Amino Acid Sequence; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009294:Narcotics / Q000138:chemical synthesis / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D012996:Solutions
chemical_list: D009294:Narcotics; D010456:Peptides, Cyclic; D012996:Solutions