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 0total (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 0total (H2O) calculated using the modified method was found to be more accurate in determining ΔG 0total (H2O) than the previously reported method.
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Zheng, X., Yang, B. An improved method for measuring the stability of a three-state unfolding protein. Chin. Sci. Bull. 55, 4120–4124 (2010). https://doi.org/10.1007/s11434-010-4242-9
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DOI: https://doi.org/10.1007/s11434-010-4242-9