[Fourier transform infrared spectroscopy study on the protein secondary structure of photosystem II reaction center].
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.
Lu
Wei
W
National Lab. for Infaraed Physics, Shanghai Institute of Technical Physics, Chinese Academy of Sciences, Shanghai 200083, China.
Xu
Chun-he
CH
Li
Rong
R
Chen
Zhang-hai
ZH
Yuan
Xian-zhang
XZ
Shi
Guo-liang
GL
Shen
Xue-chu
XC
Shen
Yun-gang
YG
Lu
Hong
H
D000577:Amides; D010316:Particle Size; D045332:Photosystem II Protein Complex / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D018724:Spinacia oleracea / Q000737:chemistry*
D000577:Amides; D045332:Photosystem II Protein Complex