Solvent and conformation dependence of amide I vibrations in peptides and proteins containing proline
Name
proline_map resubmit.pdf
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8.99 MB
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Adobe PDF
Checksum (MD5)
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Author(s)
Roy, Santanu
Lessing, Joshua Aaron
Ganim, Ziad
Meisl, Georg Herbert
Tokmakoff, Andrei
Knoester, Jasper
Jansen, Thomas L. C.
Date Issued
December 2011
Journal
Journal of Chemical Physics
Publisher
American Institute of Physics
Citation
Roy, Santanu et al. “Solvent and Conformation Dependence of Amide I Vibrations in Peptides and Proteins Containing Proline.” The Journal of Chemical Physics 135.23 (2011): 234507. Web.
Version
Author's final manuscript
Abstract
We present a mixed quantum-classical model for studying the amide I vibrational dynamics (predominantly CO stretching) in peptides and proteins containing proline. There are existing models developed for determining frequencies of and couplings between the secondary amide units. However, these are not applicable to proline because this amino acid has a tertiary amide unit. Therefore, a new parametrization is required for infrared-spectroscopic studies of proteins that contain proline, such as collagen, the most abundant protein in humans and animals. Here, we construct the electrostatic and dihedral maps accounting for solvent and conformation effects on frequency and coupling for the proline unit. We examine the quality and the applicability of these maps by carrying out spectral simulations of a number of peptides with proline in D2O and compare with experimental observations.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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Creative Commons Attribution-Noncommercial-Share Alike 3.0
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DOI of Published Version
https://doi.org/10.1063/1.3665417
