期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 113, 期 3, 页码 592-602出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp807528q
关键词
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资金
- National Science Foundation [CHE-0750307, CHE-0832584]
- National Institutes of Health [A1064797]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0750307] Funding Source: National Science Foundation
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.
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