Boat Conformation of cyclo-[L-Pro2-D-Pro]
✍ Scribed by Dr. Jan Willem Bats; Dipl.-Chem. Axel Friedrich; Prof. Dr. Hartmut Fuess; Prof. Dr. Horst Kessler; Dipl.-Chem. Werner Mästle; Prof. Dr. Manfred Rothe
- Publisher
- John Wiley and Sons
- Year
- 1979
- Tongue
- English
- Weight
- 260 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0044-8249
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The title compound represents the smallest member of cyclic proline peptides corresponding to the general formula c ( DDLL-Pro,), with a strictly D,D,L,L double-alternating sequence of the chiral amino acid residues. The cyclopeptides with n 2 2 could be synthesized from both DDLL-Pro4 ( 1 ) and DLL
Ulm, Federal Republic of Gennany ## Synopsis Combinations of L-and D-proline residues are useful compounds for finding new structures and properties of cyclic peptides. This is demonstrated with one striking example, the cyclic tetrapeptide ~(D-P~o-L-P~o-D-P~o-L-P~o). For this molecule composed o
The crystal structures of Bu'CO-L-Pro-L-Pro-NHMe, H 2 0 ( I : monoclinic; P2,; a = 6.662, b = 11.067, c = 12.205 A; P = 96.28") and Bu'CO-L-Pro-DPro-NHMe (2: monoclinic; P2,; a = 10.770, b = 15.039, c = 11.325 .&; p = 110.00") have been solved by x-ray diffraction. Structure 1 accommodates an open d
Cyclic octapeptides, cyclo(X-Pro)4, where X represents Phe, Leu, or Lys(Z), were synthesized and their conformations investigated. A Cz-symmetric conformer containing two cis peptide bonds was found in all of these cyclic octapeptides. The numbers of available conformations due to the cis-trans isom
The solid state conformational analysis of the ionophoric homodetic bicyclic cyclo ( Glu-Leu-Pro-Gly-Lys-Leu-Pro-G1y)cyclo ( ly-5c) Gly (BCP3) has been carried out by x-ray diffraction. It crystallizes with 4.5 molecules of water per peptide molecule in the monoclinic system, space group PZ1 with a