HYDROGEN-EXCHANGE MEASUREMENT OF THE FREE-ENERGY OF STRUCTURAL AND ALLOSTERIC CHANGE IN HEMOGLOBIN

被引：87
作者：
ENGLANDER, SW
ENGLANDER, JJ
MCKINNIE, RE
ACKERS, GK
TURNER, GJ
WESTRICK, JA
GILL, SJ
机构：
[1] UNIV COLORADO,DEPT BIOCHEM,BOULDER,CO 80309
[2] WASHINGTON UNIV,DEPT BIOCHEM & MOLEC BIOPHYS,ST LOUIS,MO 63110
来源：
SCIENCE | 1992年 / 256卷 / 5064期
关键词：
D O I：
10.1126/science.256.5064.1684
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：
The inability to localize and measure the free energy of protein structure and structure change severely limits protein structure-function investigations. The local unfolding model for protein hydrogen exchange quantitatively relates the free energy of local structural stability with the hydrogen exchange rate of concerted sets of structurally related protons. In tests with a number of modified hemoglobin forms, the loss in structural free energy obtained locally from hydrogen exchange results matches the loss in allosteric free energy measured globally by oxygen-binding and subunit dissociation experiments.
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页码：1684 / 1687
页数：4
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