Structural characteristics of two highly selective opioid peptides
β Scribed by Richard J. Knapp; Henry I. Yamamura; Wieslaw Kazmierski; Victor J. Hruby
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 527 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0265-9247
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The discovery of endogenous opioid peptides 25 years ago opened up a new chapter in efforts to understand the origins and control of pain, its relationships to other biological functions, including inflammatory and other immune responses, and the relationships of opioid peptides and their receptors
The allowed conformations of the p-receptor-selective cyclic opioid peptide analog H-Tyr-D-Om-Phe-Asp-NH, were determined using a grid search through the entire conformational space. Energy mnimization of the 13-membered ring structure lacking the exocyclic Tyr' residue and the Phe3 side chain using