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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
Fourier transform infrared spectroscopy (FTIR) was used to study the effect of β polymerization on the protein secondary structure of photosystem Ⅱ (PSⅡ) particles under high temperature conditions. The beta-polymerized samples with biologically active and high temperature proteins were all measured at room temperature by infrared spectroscopy and their Amide I absorption bands were used to quantitatively characterize the properties of the two samples. Spectral analysis was performed using a direct Lorentz linear fit, and the spectral results showed that the infrared spectrum of the secondary structure of PSⅡ would undergo a strong irreversible change after thermal denaturation at 40 ℃. However, its IR spectra can still be fitted with three Lorentz line types as the active PS II protein, showing the superiority of the FTIR infrared spectroscopy in the study of protein thermal denaturation