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| PSⅡ中蛋白二级结构中β聚合效应的红外光谱研究 | |
| 引用本文： | 陆卫,徐春和,李荣,陈张海,袁先璋,史国良,沈学础,沈允钢,陆红.PSⅡ中蛋白二级结构中β聚合效应的红外光谱研究[J].光谱学与光谱分析,2002,22(5):749-751. |
| 作者姓名： | 陆卫 徐春和 李荣 陈张海 袁先璋 史国良 沈学础 沈允钢 陆红 |
| 作者单位： | 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. 中国科学院上海技术物理研究所,红外物理国家重点实验室,上海,200083;中国科学院上海植物生理研究所,上海,200032 3. 中国科学院上海植物生理研究所,上海,200032 4. 复旦大学生物系,上海,200043 |
| 基金项目： | 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400℃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，显示了FTIR红外光谱方法在研究蛋白热变性方面的优越性。 |
| 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 |
| 文章编号： | 1000-0593(2002)05-0749-03 |
| 修稿时间： | 2001年8月11日 |
Fourier Transform Infrared Spectroscopy Study on the Protein Secondary Structure of Photosystem Ⅱ Reaction Center |
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| LU Wei ,XU Chun-he ,LI Rong ,CHEN Zhang-hai ,YUAN Xian-zhang ,SHI Guo-liang ,SHEN Xue-chu ,SHEN Yun-gang ,and LU Hong .National Lab. for Infaraed Physics.Fourier Transform Infrared Spectroscopy Study on the Protein Secondary Structure of Photosystem Ⅱ Reaction Center[J].Spectroscopy and Spectral Analysis,2002,22(5):749-751. | |
| Authors: | LU Wei XU Chun-he LI Rong CHEN Zhang-hai YUAN Xian-zhang SHI Guo-liang SHEN Xue-chu SHEN Yun-gang and LU Hong National Lab for Infaraed Physics |
| Institution: | National Lab. for Infaraed Physics, Shanghai Institute of Technical Physics, Chinese Academy of Sciences, Shanghai 200083, China. |
| Abstract: | 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 beta condensation effect is obviously characterized by infrared absorption spectra. The infrared spectra of both living protein and beta 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 beta 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. |
| Keywords: | FTIR |
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