期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 129, 期 11, 页码 3168-3172出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja066289n
关键词
-
资金
- Engineering and Physical Sciences Research Council [GR/S95510/01, GR/S75369/01] Funding Source: researchfish
Changes in the ultrafast dynamics and terahertz Raman spectrum accompanying a helix-to-coil transition of a homo-polypeptide have been observed for the first time. Formation of the alpha-helix is associated with a shift to lower frequency of a broad Raman band attributable to solvent-peptide intermolecular hydrogen bonding. This band facilitates direct spectroscopic observation of so-called hydration water near a peptide and yields the first quantitative estimate of the time scale of the ultrafast dynamics in the solvation shell, which range from 0.18 to 0.33 ps (185-100 cm(-1)) depending on the secondary structure of the peptide. Such fast motions of solvent molecules have been referred to as the lubricant of life and are thought to play key roles in determining structure and activity of proteins.
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