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

	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
	Ruan, KC; Xu, CH; Li, TT; Li, J; Lange, R; Balny, C
刊名	EUROPEAN JOURNAL OF BIOCHEMISTRY
	2003
卷号	270 期号:8 页码:1654-1661
关键词	conformational changes hydrostatic pressure spinach particle protein denaturation
通讯作者	Ruan, KC (reprint author), Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, Lab Proteom, Shanghai Inst Biol Sci, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,
英文摘要	We have studied the reaction native <-> denatured for the 33-kDa protein isolated from photosystem II. Sucrose and glycerol have profound effects on pressure-induced unfolding. The additives shift the equilibrium to the left; they also cause a significant decrease in the standard volume change (DeltaV). The change in DeltaV was related to the sucrose and glycerol concentrations. The decrease in DeltaV varied with the additive: sucrose caused the largest effect, glycerol the smallest. The theoretical shift of the half-unfolding pressure (P-1/2) calculated from the net increase in free energy by addition of sucrose and glycerol was lower than that obtained from experimental mea- surements. This indicates that the free energy change caused by preferential hydration of the protein is not the unique factor involved in the protein stabilization. The reduction in DeltaV showed a large contribution to the theoretical P-1/2 shift, suggesting that the DeltaV change, caused by the sucrose or glycerol was associated with the protein stabilization. The origin of the DeltaV change is discussed. The rate of pressure-induced unfolding in the presence of sucrose or glycerol was slower than the refolding rate although both were significantly slower than that observed without any stabilizers.
学科主题	Biochemistry & Molecular Biology
类目[WOS]	Biochemistry & Molecular Biology
关键词[WOS]	DERIVATIVE UV-SPECTROSCOPY ; HIGH HYDROSTATIC-PRESSURE ; PRION PROTEIN ; STAPHYLOCOCCAL NUCLEASE ; CONFORMATIONAL DRIFT ; OSMOTIC-STRESS ; RIBONUCLEASE-A ; WATER ; DENATURATION ; COMPRESSIBILITY
收录类别	SCI
语种	英语
WOS记录号	WOS:000182118800005
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/2339]
专题	上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式 GB/T 7714	Ruan, KC,Xu, CH,Li, TT,et al. 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[J]. EUROPEAN JOURNAL OF BIOCHEMISTRY,2003,270(8):1654-1661.
APA	Ruan, KC,Xu, CH,Li, TT,Li, J,Lange, R,&Balny, C.(2003).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.EUROPEAN JOURNAL OF BIOCHEMISTRY,270(8),1654-1661.
MLA	Ruan, KC,et al."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".EUROPEAN JOURNAL OF BIOCHEMISTRY 270.8(2003):1654-1661.