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Conformations of cyclo-l-his-l-ser, cyclo-l-his-l-asp, and cyclo-l-his-l-his

✍ Scribed by Ziauddin; K.D. Kopple; C.A. Bush

Book ID
104236425
Publisher
Elsevier Science
Year
1972
Tongue
French
Weight
202 KB
Volume
13
Category
Article
ISSN
0040-4039

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πŸ“œ SIMILAR VOLUMES

1H NMR study of cyclo-L-Thr-L-Thr and cy
1H NMR study of cyclo-L-Thr-L-Thr and cyclo-L-Thr-L-His conformations
✍ Marius Ptak; Annie Heitz πŸ“‚ Article πŸ“… 1974 πŸ› John Wiley and Sons 🌐 English βš– 191 KB

## Abstract Cyclodipeptides containing L‐Thr and L‐His residues have been studied by ^1^H NMR in D~2~O and DMSO‐__d__~6~. In the neutral form in D~2~O as in DMSO‐__d__~6~, the folded form of the L‐His residue is not unique. The diketopiperazine ring seems to be not strictly planar.

Solution conformation and hydrolytic act
Solution conformation and hydrolytic activity of cyclo(D-leu-L-His)
✍ Masao Tanihara; Yukio Imanishi; Toshinobu Higashimura πŸ“‚ Article πŸ“… 1977 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 631 KB

## Abstract It has been reported previously that a cyclic dipeptide, cyclo(D‐Leu‐L‐His), showed a high hydrolytic activity toward a hydrophobic ester, __p__‐nitrophenyl laurate. In order to determine the reason for the high catalytic activity, the conformation of cyclo(D‐Leu‐L‐His) in aqueous solut