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.
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 a-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.
出处
《高等学校化学学报》
SCIE
EI
CAS
CSCD
北大核心
2007年第12期2255-2258,共4页
Chemical Journal of Chinese Universities
基金
国家自然科学基金重点项目(批准号:30227002)资助
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
Infrared spectroscopy
Window factor analysis（WFA）
Heating
Bovine serum albumin（BSA）
Secondary structure
