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- W2086688377 abstract "We have shown (J. Phys. Chem. A 2004, 108, 10923; 2007, 111, 5300) that the CαDα stretch frequency, ν(CD), can discriminate between uniform αR, β, and polyproline II conformations of isolated peptides. Similar results for such peptides to which explicit waters are hydrogen bonded exhibit shifts in ν(CD) from those of the isolated structures. We demonstrate that the main source of these frequency shifts is the formation of Cα−Dα···O hydrogen bonds to water. Taking into account C−H···O(water) hydrogen bonding, together with the traditional bonding of peptide groups to water, can be expected to increase our understanding of the interaction of proteins with their aqueous environment." @default.
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- W2086688377 date "2008-11-01" @default.
- W2086688377 modified "2023-09-25" @default.
- W2086688377 title "Peptide C<sup>α</sup>D<sup>α</sup> Stretch Frequencies in a Hydrated Conformation Are Perturbed Mainly by C<sup>α</sup>−D<sup>α</sup>···O Hydrogen Bonding" @default.
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- W2086688377 doi "https://doi.org/10.1021/jp808515t" @default.
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