Abstract
The conformation of a new Tyr-c[Lys-Phe-Asp]-NH 2 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 possessses significant orientational freedom.
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