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• W2094670978 abstract "The amide I vibrational mode, primarily associated with peptide-bond carbonyl stretches, has long been used to probe the structures and dynamics of peptides and proteins by infrared (IR) spectroscopy. A number of ab initio-based amide I vibrational frequency maps have been developed for calculating IR line shapes. In this paper, a new empirical amide I vibrational frequency map is developed. To evaluate its performance, we applied this map to a system of isotope-edited CD3-zeta membrane peptide bundles in aqueous solution. The calculated 2D-IR diagonal line widths vary from residue to residue and show an asymmetric pattern as a function of position in the membrane. The theoretical results are in fair agreement with experiments on the same system. Through analysis of the computed frequency time-correlation functions, it is found that the 2D-IR diagonal widths are dominated by contributions from the inhomogeneous frequency distributions, from which it follows that these widths are a good probe of the extent of local structural fluctuations. Thus, the asymmetric pattern of line widths follows from the asymmetric structure of the bundle in the membrane." @default.
• W2094670978 created "2016-06-24" @default.
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• W2094670978 creator A5032907309 @default.
• W2094670978 creator A5089989500 @default.
• W2094670978 date "2008-11-17" @default.
• W2094670978 modified "2023-10-01" @default.
• W2094670978 title "Empirical Amide I Vibrational Frequency Map: Application to 2D-IR Line Shapes for Isotope-Edited Membrane Peptide Bundles" @default.
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• W2094670978 doi "https://doi.org/10.1021/jp807528q" @default.
• W2094670978 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2633092" @default.
• W2094670978 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19053670" @default.
• W2094670978 hasPublicationYear "2008" @default.
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