The thermodynamic analysis of protein stabilization by sucrose and glycerol against pressure-induced unfolding. The typical example of the 33-kDa protein from spinach photosystem II
作者： Kangcheng Ruan , Chunhe Xu , Tingting Li , Jiong Li , Reinhard Lange
DOI: 10.1046/J.1432-1033.2003.03485.X
关键词: Hydrostatic pressure 、 Protein stabilization 、 Biophysics 、 Sucrose 、 Chromatography 、 Gibbs free energy 、 Glycerol 、 Chemistry 、 Volume change 、 Photosystem II 、 Cell biology 、 Biochemistry 、 Molecular biology
摘要: We have studied the reaction native denatured for 33-kDa protein isolated from photosystem II. Sucrose and glycerol profound effects on pressure-induced unfolding. The additives shift equilibrium to left; they also cause a significant decrease in standard volume change (DeltaV). DeltaV was related sucrose concentrations. varied with additive: caused largest effect, smallest. theoretical of half-unfolding pressure (P-1/2) calculated net increase free energy by addition lower than that obtained experimental mea- surements. This indicates preferential hydration is not unique factor involved stabilization. reduction showed large contribution P-1/2 shift, suggesting change, or associated origin discussed. rate unfolding presence slower refolding although both were significantly observed without any stabilizers.
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