Conformation of a cyclic opioid peptide analog by NMR and molecular dynamics simulation.
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.
Chuang
L C
LC
Chemistry Department, National Tsing Hua University, Hsinchu, Taiwan.
Chen
S T
ST
Ya
C
C
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
D009294:Narcotics; D010456:Peptides, Cyclic; D012996:Solutions