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

被引：4
|
作者：
Zheng XiaoYan [1 ]
Yang BinSheng [1 ]
机构：
[1] Shanxi Univ, Inst Mol Sci, Key Lab Chem Biol & Mol Engn, Minist Educ, Taiyuan 030006, Peoples R China
来源：
CHINESE SCIENCE BULLETIN | 2010年 / 55卷 / 36期
基金：
中国国家自然科学基金;
关键词：
protein stability; three-state model; Y79W-W83F; unfolding; GUANIDINE-HYDROCHLORIDE; ALPHA-CHYMOTRYPSIN; UREA; DENATURATION; THERMODYNAMICS; ENERGY; COPC;
D O I：
10.1007/s11434-010-4242-9
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
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 [Delta G(total)(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 Delta G(total)(0)(H2O) calculated using the modified method was found to be more accurate in determining Delta G(total)(0)(H2O) than the previously reported method.
引用
收藏
页码：4120 / 4124
页数：5
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