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Heat Denaturation of Protein Structures and Chlorophyll States in PSII Membranes
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作者 李冬海 阮翔 +4 位作者 许强 王可玢 公衍道 匡廷云 赵南明 《Tsinghua Science and Technology》 SCIE EI CAS 2002年第4期407-410,共4页
Heat denaturation is an important technique in the study of the structure and function of photosynthetic proteins. Heat denaturation of photosystem II (PSII) membrane was studied using circular dichroism (CD) spect... Heat denaturation is an important technique in the study of the structure and function of photosynthetic proteins. Heat denaturation of photosystem II (PSII) membrane was studied using circular dichroism (CD) spectroscopy, differential scanning calorimetry (DSC) and oxygen electrode. Complete loss of oxygen evolving activity of the PSII membrane was observed at temperatures below 45℃ . The decrease of excitonic interaction between chlorophyll molecules occurred more rapidly than the change of the protein secondary structure of the PSII membrane at temperatures above 45℃ . The results indicate that the protein secondary structure of the membrane proteins in PSII membranes is more stable than the excitonic interaction between chlorophyll molecules during heat denaturation. 展开更多
关键词 photosystem II (PSII) oxygen evolving activity circular dichroism (CD) differential scanning calorimetry (DSC) excitonic interaction heat denaturation
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