PSⅡ中蛋白二級結構中β聚合效應的紅外光譜研究

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

陸衛(Wei Lu)；徐春和(Chun-He Xu)；李榮(Rong Li)；陳張海(Zhang-Hai Chen)；袁先璋(Xian-Zhang Yuan)；史國良(Guo-Liang Shi)；沈學礎(Xue-Chu Shen)；沈允鋼(Yun-Gang Shen)；陸紅(Hong Lu)

光系統Ⅱ ； 蛋白二級結構 ； FTIR ； Photosystem Ⅱ ； Protein secondary structure ； FTIR

光譜學與光譜分析

22卷5期（2002 / 10 / 01）

749 - 751

簡體中文

利用Fourier變換紅外光諳(FTLR)方法研究了光系統Ⅱ(PSⅡ)膜顆粒中蛋白二級結構在高溫條件下的β聚合效應。具有生物活性的高溫蛋白的β聚合樣品的紅外光譜測量溫度均是室溫，它們的酰胺Ⅰ吸收帶被用來對兩種樣品的特性進行定量的分析。光譜的分析方法採用了直接Lorentz線型擬合，光譜結果表明光系統Ⅱ二級結構在400℃下發生熱變性後，其紅外光譜將發生很強的不可逆的變化。但其紅外光譜與活性PSⅡ蛋白一樣仍可用3個Lorentz線型擬合,顯示了FTIR紅外光譜方法在研究蛋白熱性方面的優越性。

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 of both living protein and β condensed protein samples are measured at room temperature. The amide Ⅰ band in infrared spectrum in 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.