1. [Fourier transform infrared spectroscopy study on the protein secondary structure of photosystem II reaction center].
- Author
-
Lu W, Xu CH, Li R, Chen ZH, Yuan XZ, Shi GL, Shen XC, Shen YG, and Lu H
- Subjects
- Amides, Particle Size, Protein Structure, Secondary, Photosystem II Protein Complex chemistry, Spectroscopy, Fourier Transform Infrared, Spinacia oleracea chemistry
- 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.
- Published
- 2002