Pressure equilibrium and jump study on unfolding of 23-kDa protein from spinach photosystem II
文献类型:期刊论文
作者 | Tan, CY; Xu, CH; Wong, J; Shen, JR; Sakuma, S; Yamamoto, Y; Lange, R; Balny, C; Ruan, KC |
刊名 | BIOPHYSICAL JOURNAL
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出版日期 | 2005 |
卷号 | 88期号:2页码:1264-1275 |
通讯作者 | Ruan, KC (reprint author), Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,balny@monpt.inserm.fr ; kcruan@sibs.ac.cn |
英文摘要 | Pressure-induced unfolding of 23-kDa protein from spinach photosystem II has been systematically investigated at various experimental conditions. Thermodynamic equilibrium studies indicate that the protein is very sensitive to pressure. At 20 degreesC and pH 5.5, 23-kDa protein shows a reversible two-state unfolding transition under pressure with a midpoint near 160 MPa, which is much lower than most natural proteins studied to date. The free energy (DeltaG(u)) and volume change (DeltaV(u)) for the unfolding are 5.9 kcal/mol and - 160 ml/mol, respectively. It was found that NaCl and sucrose significantly stabilize the protein from unfolding and the stabilization is associated not only with an increase in DeltaG(u) but also with a decrease in DeltaV(u). The pressure-jump studies of 23-kDa protein reveal a negative activation volume for unfolding ( - 66.2 ml/mol) and a positive activation volume for refolding (84.1 ml/mol), indicating that, in terms of system volume, the protein transition state lies between the folded and unfolded states. Examination of the temperature effect on the unfolding kinetics indicates that the thermal expansibility of the transition state and the unfolded state of 23-kDa protein are closer to each other and they are larger than that of the native state. The diverse pressure-refolding pathways of 23-kDa protein in some conditions were revealed in pressure-jump kinetics. |
学科主题 | Biophysics |
类目[WOS] | Biophysics |
关键词[WOS] | TRANSFORM INFRARED-SPECTROSCOPY ; DERIVATIVE UV-SPECTROSCOPY ; NUCLEAR-MAGNETIC-RESONANCE ; HIGH HYDROSTATIC-PRESSURE ; OXYGEN-EVOLVING COMPLEX ; X-RAY-SCATTERING ; STAPHYLOCOCCAL NUCLEASE ; DENATURED STATE ; FOLDING REACTIONS ; TRANSITION-STATE |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000226750800043 |
版本 | 出版稿 |
源URL | [http://202.127.25.143/handle/331003/1867] ![]() |
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 | Tan, CY,Xu, CH,Wong, J,et al. Pressure equilibrium and jump study on unfolding of 23-kDa protein from spinach photosystem II[J]. BIOPHYSICAL JOURNAL,2005,88(2):1264-1275. |
APA | Tan, CY.,Xu, CH.,Wong, J.,Shen, JR.,Sakuma, S.,...&Ruan, KC.(2005).Pressure equilibrium and jump study on unfolding of 23-kDa protein from spinach photosystem II.BIOPHYSICAL JOURNAL,88(2),1264-1275. |
MLA | Tan, CY,et al."Pressure equilibrium and jump study on unfolding of 23-kDa protein from spinach photosystem II".BIOPHYSICAL JOURNAL 88.2(2005):1264-1275. |
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