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 co...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.展开更多
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)
文摘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.
