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机构地区:[1]中国科学技术大学合肥微尺度物质科学国家实验室,化学物理系,合肥230026 [2]西安电子科技大学物理与光电工程学院,西安710071 [3]量子信息与量子科技前沿协同创新中心,合肥230026
出 处:《Chinese Journal of Chemical Physics》2016年第1期129-134,I0002,共7页化学物理学报(英文)
基 金:This work was supported by the National Natural Science Foundation of China (No.91127042, No.21103158, No.21273211, No.21473171), the National Key Basic Research Special Foundation (No.2013CB834602 and No.2010CB923300), the Fundamental Research Funds for the Central Universities (No.7215623603), and the Hua-shan Mountain Scholar Program. We also thank Doctor Kang-zhen Tian and Professor Shu-ji Ye for the measurement of IR spectra of aqueous lysozyme.
摘 要:The amide A band of protein is sensitive to the hydrogen bands of amide groups of proteins. However, it is hard to distinguish the amide A band of aqueous protein in situ directly, since it overlaps with O-H stretching vibration of water. In this work, we presented a new analytical method of Raman ratio spectrum, which can extract the amide A band of proteins in water. To obtain the Raman ratio spectrum, the Raman spectrum of aqueous protein was divided by that of pure water. A mathematical simulation was employed to examine whether Raman ratio spectrum is effective. Two kinds of protein, lysozyme and (^-chymotrypsin were employed. The amide A bands of them in water were extracted from Raman ratio spectra. Additionally, the process of thermal denaturation of lysozyme was detected from Raman ratio spectrum. These results demonstrated the Raman ratio spectra could be employed to study the amide A modes of proteins in water.
关 键 词:Raman ratio spectrum. Amide A band. In situ Protein WATER
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