A systematic survey has been made, using molecular mechanics, of the conformation of cycle(-NY-Mabu-Gly-Ala-Ala-), where Mabu is (R)-a-methyl-y-arninobutyric acid. This molecule corresponds to the 14-membered ring of the conformationally restricted, biologically active, Leu-enkephalin analog, Tyr-~~
Conformation of cyclic analogs of enkephalin. II. Analogs containing a cystine bridge
โ Scribed by David Hall; Nicola Pavitt
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1984
- Tongue
- English
- Weight
- 416 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
โฆ Synopsis
A systematic survey has been made, using molecular mechanics, of the conformation of the ring entity of the enkephalin analogs, [~Cys~-~-Cys~]enkephalinamide and [D Cys2-~Cys5]enkephalinamide. These molecules are considerably more flexible than the analog Tyr-cyclo(Ny-DA,bu-Gly-Phe-Leu-), but the favored conformations of all three are very similar. The results of these studies are compatible with a Gly3-Phe' type II' bend in the active conformation of enkephalin.
๐ SIMILAR VOLUMES
## Synopsis A comparative study has been made using molecular mechanics of the ring entity of the active enkephalin analogs, Tyr-cyclo(-N'-D-XXX-Gly-Phe-Leu-), where XXX is variously A,pr, A,bu, and Orn. Several conformations are favored for all three, and the lower-energy models are compatible wi
We report the conformational analysis by 1 H-NMR in DMSO and computer simulations involving distance geometry and molecular dynamics simulations of peptoid analogs of the cyclic hexapeptide c-[Phe 11 -Pro 6 -Phe 7 -D-Trp 8 -Lys 9 -Thr 10 ] L-363,301 (the numbering refers to the positions in native s
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
The Cu(I1) binding site of human serum albumin is located on the N-terminal sequence Asp-Ala-His.l-4 It has been shown that the synthetic tripeptide Asp-Ala-His N-methylamide exhibits an affinity towards Cu(I1) ions even higher than that of serum albumin itself.5 In general, i t has been observed th