0000000001266251
AUTHOR
M. Rospenk
Combined effect of the DeltaPhe or DeltaAla residue and the p-nitroanilide group on a didehydropeptides conformation.
Two series of dehydropeptides of the general formulae Boc-Gly-X-Phe-p-NA, Boc-Gly-Gly-X-Phe-p-NA, Gly-X-Gly-Phe-p-NA·TFA, and Boc-Gly-X-Gly-Phe-p-NA, with X = ΔZPhe and ΔAla, were studied with NMR in DMSO and CDCl3-DMSO, and with CD in MeOH, MeCN, and TFE. The NMR spectra measured in DMSO suggest that peptides with the ΔPhe residue next to Phe are folded whereas peptides with Gly between ΔPhe and Phe are less ordered. NMR spectra of ΔAla-containing peptides indicate that these peptides are flexible and their conformational equilibria are populated by many different conformations. The CD spectra show that conformational properties of the peptides studied are distinctly influenced by a mutual…
CCDC 619860: Experimental Crystal Structure Determination
Related Article: M.Lisowski, R.Latajka, B.Picur, T.Lis, I.Bryndal, M.Rospenk, M.Makowski, P.Kafarski|2008|Biopolymers|89|220|doi:10.1002/bip.20897
CCDC 619859: Experimental Crystal Structure Determination
Related Article: M.Lisowski, R.Latajka, B.Picur, T.Lis, I.Bryndal, M.Rospenk, M.Makowski, P.Kafarski|2008|Biopolymers|89|220|doi:10.1002/bip.20897
CCDC 619858: Experimental Crystal Structure Determination
Related Article: M.Lisowski, R.Latajka, B.Picur, T.Lis, I.Bryndal, M.Rospenk, M.Makowski, P.Kafarski|2008|Biopolymers|89|220|doi:10.1002/bip.20897