【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 ,显示了FTIR红外光谱方法在研究蛋白热变性方面的优越性更多还原

【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 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.更多还原