期刊
ANNUAL REVIEW OF PHYSICAL CHEMISTRY, VOL 69
卷 69, 期 -, 页码 253-271出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-physchem-052516-045011
关键词
electric fields; infrared spectroscopy; protein-protein interactions; protein electrostatics; membrane biophysics
Measurement of the electrostatic interactions that give rise to biological functions has been a longstanding challenge in biophysics. Advances in spectroscopic techniques over the past two decades have allowed for the direct measurement of electric fields in a wide variety of biological molecules and systems via the vibrational Stark effect (VSE). The frequency of the nitrile stretching oscillation has received much attention as an electric field reporter because of its sensitivity to electric fields and its occurrence in a relatively transparent region of the infrared spectrum. Despite these advantages and its wide use as a VSE probe, the nitrile stretching frequency is sensitive to hydrogen bonding in a way that complicates the straightforward relationship between measured frequency and environmental electric field. Here we highlight recent applications of nitrile VSE probes with an emphasis on experiments that have helped shape our understanding of the determinants of nitrile frequencies in both hydrogen bonding and nonhydrogen bonding environments.
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