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Conformation dependence of the C α D α stretch mode in peptides: Side‐chain influence in dipeptide structures
Author(s) -
Mirkin Noemi G.,
Krimm Samuel
Publication year - 2010
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.21523
Subject(s) - side chain , chemistry , preprint , dipeptide , peptide , homogeneous , aqueous solution , alanine , stereochemistry , amino acid , chemical physics , organic chemistry , thermodynamics , physics , polymer , biochemistry , quantum mechanics
We have shown by theoretical studies of alanine peptides that the C α D α stretch frequency could be particularly useful for determining peptide structure because of its sensitivity to the φ,ψ torsion angles at the C α atom. To demonstrate that this is a robust methodology worthy of experimental exploration, we have also shown that this mode is even more determinative of conformation in aqueous solution, mainly as a result of the development of differential C α D α ···O(water) interactions. As further assurance, we now determine the influence of the side chain on this band, showing for aliphatic, a polar, and an aromatic side chains that the dependence is minor and explaining why this is also expected for other side chains. These results should stimulate new experimental methodologies in the field of peptide structure determination. © 2010 Wiley Periodicals, Inc. Biopolymers 93: 1065–1071, 2010. 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