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作 者:ZHENG XiaoYan YANG BinSheng
出 处:《Chinese Science Bulletin》2010年第36期4120-4124,共5页
基 金:supported by the National Natural Science Foundation of China (20771068 and 20901048);the Ph.D. Programs Foundation of the Ministry of Education of China (20091401110007);the Natural Sci-ence Foundation of Shanxi Province (2010011011-1)
摘 要:In the current three-state protein unfolding model, the two transitions are considered to be independent and each transition is fitted to a two-state unfolding model. This three-state unfolding process is therefore composed of two sequential two-state unfolding processes. In this paper, a modified method is presented to determine the value of the unfolding free energy [Gt0otal(H2O)] for the three-state unfolding equilibrium of proteins. This method is demonstrated on the apoCopC protein mutant, Y79W-W83F-Cu, which unfolds via a three-state process. The value of Gt0otal(H2O) calculated using the modified method was found to be more accurate in determining Gt0otal(H2O) than the previously reported method.In the current three-state protein unfolding model, the two transitions are considered to be independent and each transition is fitted to a two-state unfolding model. This three-state unfolding process is therefore composed of two sequential two-state unfolding processes. In this paper, a modified method is presented to determine the value of the unfolding free energy [△Gtotal^0(H2O)] for the three-state unfolding equilibrium of proteins. This method is demonstrated on the apoCopC protein mutant, Y79W-W83F-Cu, which unfolds via a three-state process. The value of △Gtotal^0(H2O) calculated using the modified method was found to be more accurate in determining △Gtotal^0(H2O) than the previously reported method.
关 键 词:蛋白质 三态 稳定 测量 平衡状态 突变体 C蛋白 模型
分 类 号:Q51[生物学—生物化学] TN79[电子电信—电路与系统]
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