An improved method for measuring the stability of a three-state unfolding protein |
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Authors: | XiaoYan Zheng BinSheng Yang |
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Institution: | 1.Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education,Shanxi University,Taiyuan,China |
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Abstract: | 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 δG
total0(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 ΔG
total0(H2O) calculated using the modified method was found to be more accurate in determining ΔG
total0(H2O) than the previously reported method. |
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Keywords: | |
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