An improved method for measuring the stability of a three-state unfolding protein

作者：Zheng XiaoYan; Yang BinSheng^*

来源：Chinese Science Bulletin, 2010, 55(36): 4120-4124.

DOI：10.1007/s11434-010-4242-9

• protein stability
• three-state model
• Y79W-W83F
• unfolding

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 [Delta G(total)(0)(H(2)O)] 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 Delta G(total)(0)(H(2)O) calculated using the modified method was found to be more accurate in determining Delta G(total)(0)(H(2)O) than the previously reported method.

• 出版日期2010-12
• 单位山西大学