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RESEARCH PRODUCT

Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 2 and 5 in peptide chain

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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 310-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