作者
Sayan Bagchi, Stephen D Fried, Steven G Boxer
发表日期
2012/6/27
期刊
Journal of the American Chemical Society
卷号
134
期号
25
页码范围
10373-10376
出版商
American Chemical Society
简介
Electrostatic interactions provide a primary connection between a protein’s three-dimensional structure and its function. Infrared probes are useful because vibrational frequencies of certain chemical groups, such as nitriles, are linearly sensitive to local electrostatic field and can serve as a molecular electric field meter. IR spectroscopy has been used to study electrostatic changes or fluctuations in proteins, but measured peak frequencies have not been previously mapped to total electric fields, because of the absence of a field-frequency calibration and the complication of local chemical effects such as H-bonds. We report a solvatochromic model that provides a means to assess the H-bonding status of aromatic nitrile vibrational probes and calibrates their vibrational frequencies to electrostatic field. The analysis involves correlations between the nitrile’s IR frequency and its 13C chemical shift, whose observation is …
学术搜索中的文章
S Bagchi, SD Fried, SG Boxer - Journal of the American Chemical Society, 2012