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An improved method for measuring the stability of a three-state unfolding protein 被引量:1

An improved method for measuring the stability of a three-state unfolding protein
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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.
出处 《Chinese Science Bulletin》 SCIE EI CAS 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)
关键词 蛋白质 三态 稳定 测量 平衡状态 突变体 C蛋白 模型 protein stability, three-state model, Y79W-W83F, unfolding
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