DENATURANT M-VALUES AND HEAT-CAPACITY CHANGES - RELATION TO CHANGES IN ACCESSIBLE SURFACE-AREAS OF PROTEIN UNFOLDING

被引:1701
作者
MYERS, JK
PACE, CN
SCHOLTZ, JM
机构
[1] TEXAS A&M UNIV, DEPT MED BIOCHEM & GENET, COLLEGE STN, TX 77843 USA
[2] TEXAS A&M UNIV, DEPT BIOCHEM & BIOPHYS, COLLEGE STN, TX 77843 USA
[3] TEXAS A&M UNIV, CTR MACROMOLEC DESIGN, COLLEGE STN, TX 77843 USA
关键词
DENATURATION; GUANIDINE HYDROCHLORIDE; HEAT CAPACITY CHANGES; M VALUES; PROTEIN FOLDING; PROTEIN STABILITY; SOLVENT-ACCESSIBLE SURFACE AREA; UREA;
D O I
10.1002/pro.5560041020
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Denaturant m values, the dependence of the free energy of unfolding on denaturant concentration, have been collected for a large set of proteins. The PPI value correlates very strongly with the amount of protein surface exposed to solvent upon unfolding, with linear correlation coefficients of R = 0.84 for urea and R = 0.87 for guanidine hydrochloride. These correlations improve to R = 0.90 when the effect of disulfide bonds on the accessible area of the unfolded protein is included. A similar dependence on accessible surface area has been found previously for the heat capacity change (Delta C-p), which is confirmed here for our set of proteins. Denaturant m values and heat capacity changes also correlate well with each other. For proteins that undergo a simple two-state unfolding mechanism, the amount of surface exposed to solvent upon unfolding is a main structural determinant for both m values and Delta C-p.
引用
收藏
页码:2138 / 2148
页数:11
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