| Autor: |
E, Trzepałka, W, Kowalczyk, B, Lammek |
| Rok vydání: |
2004 |
| Předmět: |
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| Zdroj: |
The journal of peptide research : official journal of the American Peptide Society. 63(4) |
| ISSN: |
1397-002X |
| Popis: |
Two cyclic analogs of vasopressin, -Pro-Arg-Gly-NH(2) (1) and -Pro-Arg-Gly-NH(2) (2) were synthesized by the solid phase method. Their structure was determined in aqueous solution by two-dimensional NMR techniques and simulated annealing algorithm from an extended template in X-PLOR. The total chemical shift correlation spectroscopy and rotating-frame Overhauser enhancement spectroscopy of the peptides displayed four distinct sets of residual proton resonances. This suggests that both analogs adopt four families of conformations in H(2)O/D(2)O (9 : 1) (one major and three minor species). In further analysis only signals of major species (M) and of one minor species (m(1)) were considered. The major species of both peptides include a trans peptide bond between the first and second residue, and a cis form between the second and third residue. In the minor species, all peptide bonds were found to exist in trans geometry. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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