The Strength with Which a Peptide Group Can Form a Hydrogen Bond Varies with the Internal Conformation of the Polypeptide Chain
Document Type
Article
Journal/Book Title
Journal of Physical Chemistry B
Publication Date
2007
Publisher
American Chemical Society
Volume
111
Issue
38
First Page
11312
Last Page
11317
Abstract
The strength of the H-bond formed between a dipeptide and a proton acceptor molecule is assessed by correlated ab initio quantum calculations for a broad range of different conformations of the dipeptide. The H-bond energy is very sensitive to the internal (φ,ψ) angles, even when the geometry of the H-bond does not vary significantly from one conformation to another. This result indicates that the peptide NH is a much less potent proton donor in certain conformations than in others. In particular, extended conformations of a polypeptide are capable of only weak H-bonds. Thus, the interstrand NH···O H-bonds in parallel and antiparallel β-sheets are expected to be significantly weaker than those found in other conformations, such as helices, ribbons, and β-bends, even if the H-bond geometries are similar.
Recommended Citation
The Strength with Which a Peptide Group Can Form a Hydrogen Bond Varies with the Internal Conformation of the Polypeptide Chain S. Scheiner J. Phys. Chem. B 2007 111 11312-11317
Comments
Originally published by American Chemical Society in the Journal of Physical Chemistry.
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