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利用红外光谱和窗口因子分析研究加热导致的牛血清白蛋白的二级结构变化
引用本文:袁波,严惠民.利用红外光谱和窗口因子分析研究加热导致的牛血清白蛋白的二级结构变化[J].高等学校化学学报,2007,28(12):2255-2258.
作者姓名:袁波  严惠民
作者单位:浙江大学现代光学仪器国家重点实验室,国家光学仪器工程技术研究中心,杭州,310027
基金项目:国家自然科学基金重点项目
摘    要:用红外光谱和窗口因子分析(WFA)对加热导致的D2O中牛血清白蛋白(BSA)的二级结构变化进行了研究. 常规光谱分析和WFA的结果表明, BSA的结构变化开始于56 ℃, 而二级结构的剧烈变化发生在68~82 ℃, 与α-螺旋片断相连的短链变化发生的温度比其它二级结构变化的发生温度低10 ℃左右. 研究结果表明, WFA在解析溶液里蛋白质的温度相关红外光谱中起重大作用.

关 键 词:红外光谱  窗口因子分析  加热  牛血清白蛋白  二级结构
文章编号:0251-0790(2007)12-2255-04
收稿时间:2007-07-02
修稿时间:2007年7月2日

Heat-Induced Changes of Secondary Structures of BSA in D2O Studied by Infrared Spectroscopy and Window Factor Analysis
YUAN Bo,YAN Hui-Min.Heat-Induced Changes of Secondary Structures of BSA in D2O Studied by Infrared Spectroscopy and Window Factor Analysis[J].Chemical Research In Chinese Universities,2007,28(12):2255-2258.
Authors:YUAN Bo  YAN Hui-Min
Institution:State Key Laboratory of Modern Optical Instrumentation, CNERC for Optical Instrument, Zhejiang University, Hangzhou 310027, China
Abstract:Heat-induced changes of secondary structures of bovine serum albumin(BSA) in D2O was studied by using infrared spectroscopy and window factor analysis(WFA). The results obtained from the conventional spectral analysis methods and WFA indicate that conformational changes of BSA began at 56 ℃, while the drastic variations of secondary structures occurred in the temperature range of 68—82 ℃. Additionally, the temperature at which the variation of short-segment chains connecting α-helical segment took place is lower by round 10 ℃ than that of the other secondary structures. The present study reveals that WFA plays a key role in the analysis the temperature-dependent infrared spectra of protein in solution.
Keywords:Infrared spectroscopy  Window factor analysis(WFA)  Heating  Bovine serum albumin(BSA)  Secondary structure
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