PSⅡ中蛋白二级结构中β聚合效应的红外光谱研究  

Fourier Transform Infrared Spectroscopy Study on the Protein Secondary Structure of Photosystem Ⅱ Reaction Center

作　　者：陆卫[1] 徐春和 李荣[2] 陈张海[1] 袁先璋[1] 史国良[1] 沈学础[1] 沈允钢[2] 陆红[3] 

机构地区：[1]中国科学院上海技术物理研究所,红外物理国家重点实验室,上海200083 [2]中国科学院上海植物生理研究所,上海200032 [3]复旦大学生物系,上海200043

出　　处：《光谱学与光谱分析》2002年第5期749-751,共3页Spectroscopy and Spectral Analysis

基　　金：国家自然科学基金;中国科学院上海分院择优基金资助

摘　　要：利用Fourier变换红外光谱 (FTIR)方法研究了光系统Ⅱ (PSⅡ )膜颗粒中蛋白二级结构在高温条件下的 β聚合效应。具有生物活性和高温蛋白的 β聚合样品的红外光谱测量温度均是室温 ,它们的酰胺Ⅰ吸收带被用来对两种样品的特性进行定量的分析。光谱的分析方法采用了直接Lorentz线型拟合 ,光谱结果表明光系统Ⅱ二级结构在 40 0℃下发生热变性后 ,其红外光谱将发生很强的不可逆的变化。但其红外光谱与活性PSⅡ蛋白一样仍可用 3个Lorentz线型拟合 。A successful study on the secondary structure of the isolated photosystem Ⅱ (PSⅡ) particles with the Fourier transform infrared spectroscopy is reported in this paper.The β condensation effect is obviously charactetized by infrared absorption spectra.The infrared spectra of both living protein and β condensed protein samples are measured at room temperature.The amide Ⅰ band in infrared spectrum is used to perform the quantitative analysis of the sample properties.The recorded spectra show the irreversible effect for the PSⅡ particles after the 400 K heating.A rather strong change of the infrared spectra is observed due to the β condensation of PSⅡ protein.All the spectra are well fitted by 3-Lorentz-peak.The FTIR spectroscopy shows its effectiveness in studying the heating effect on the PSⅡ particles.

关 键 词：PSⅡ 二级结构 β聚合效应 红外光谱 光系统Ⅱ FTIR 蛋白质 植物 光合反应中心 分析 

分 类 号：Q945.11[生物学—植物学] Q518.1