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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
[Effects of ultraviolet-B radiation on protein structure in PS II using Fourier transform infrared spectroscopy]
Xiao Liu1, Weng-Ting Tang, Qian Li
1Key Laboratory of Resource Biology and Biotechnology in Western China, Ministry of Education, Northwest University, Xi'an 710069, China. liuxiao@nwu.edu.cn
Abstract:
The effects of ultraviolet-B (UV-B) radiation on protein structure in photosystem II (PS II) was studied using Fourier transform infrared spectroscopy. The results demonstrated that irradiation of the plant with enhanced UV-B caused the change in the structures of protein in PSII. The intensity of alpha-helix, beta-sheet was increased, while the intensity of beta-turn was decreased. The coupling of those structures with surrounding became weaker with UV-B radiation. Otherwise, the UV-B influenced the structure of tyrosine residue and made the polarity of tyrosine decrease. The changes caused by UV-B radiation could alter the combination between Mn cluster and pigments with protein inevitably. It would lead to a series of changes, such as the process of light transmission and conversion, electron transfer and oxygen evolution.
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