Premium
Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 2 and 5 in peptide chain
Author(s) -
Latajka Rafal,
Jewginski Michal,
Makowski Maciej,
Krezel Artur,
Paluch Slawomir
Publication year - 2008
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20994
Subject(s) - chemistry , peptide , chain (unit) , stereochemistry , cyclic peptide , biochemistry , physics , astronomy
Conformational preferences of a group of hexapeptides containing two dehydroamino acid residues in Positions 2 and 5 in peptide chain were investigated by means of spectroscopic methods (NMR and CD) and theoretical calculations. In the case of dimethylsulfoxide (DMSO) solution, only peptide with free N‐termini adopted rigid 3 10 ‐helical conformation, for the rest of examined peptides extended and “zig‐zag” conformers were predominant. CD measurements showed that only in chloroform solution the conformational freedom of investigated peptides was restricted. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 691–699, 2008. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com