Cis/trans conformational equilibrium across the N-methylphenylalanine2- N-methylphenylalanine3 peptide bond of arginine vasopressin analogs

Autor:	E. Trzepałka, Wioleta Kowalczyk, Bernard Lammek
Rok vydání:	2004
Předmět:	Residue (chemistry) X-PLOR Endocrinology Aqueous solution Stereochemistry Chemistry Peptide bond Nuclear magnetic resonance spectroscopy Biochemistry Two-dimensional nuclear magnetic resonance spectroscopy Cis trans isomerization Cis–trans isomerism
Zdroj:	Journal of Peptide Research. 63:333-346
ISSN:	1399-3011 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:	https://explore.openaire.eu/search/publication?articleId=doi_________::8eb83c5eeae30ad276dd456c9fb7e6cf https://doi.org/10.1111/j.1399-3011.2004.00103.x Zobrazit plný text záznamu Plný text ve formátu PDF