期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 116, 期 31, 页码 9387-9395出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp305083t
关键词
-
资金
- NIH [GM 25158]
The imidazole side-chains of histidine residues perform key roles in proteins, and spectroscopic markers are of great interest. The imidazole Raman spectrum is subject to resonance enhancement at UV wavelengths, and a number of UVRR markers of structure have been investigated. We report a systematic experimental and computational study of imidazole UVRR spectra, which elucidates the band pattern, and the effects of protonation and deprotonation, of H/D exchange, of metal complexation, and of addition of a methyl substituent, modeling histidine itself. A consistent assignment scheme is proposed, which permits tracking of the bands through these chemical variations. The intensities are dominated by normal mode contributions from stretching of the strongest ring bonds, C2N and C4C5, consistent with enhancement via resonance with a dominant imidazole pi-pi* transition.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据