APPLICATION OF LINEAR FREE-ENERGY RELATIONS TO PROTEIN CONFORMATIONAL-CHANGES - THE QUATERNARY STRUCTURAL-CHANGE OF HEMOGLOBIN

被引：74

作者：

EATON, WA

HENRY, ER

HOFRICHTER, J

机构：

[1] Laboratory of Chemical Physics, National Institute of Diabetes, National Institutes of Health, Bethesda

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 10期

关键词：

KINETICS; DYNAMICS; TRANSITION STATE THEORY; REACTION PATH; ALLOSTERY;

D O I：

10.1073/pnas.88.10.4472

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 transition state for the R arrow pointing right over arrow pointing left T quaternary conformational change of hemoglobin has thermodynamic properties much closer to those of the R conformation than to those of the T conformation. This finding is based on a comparison of activation and equilibrium enthalpy and entropy changes and on the observation of a linear free energy relationship between quaternary rate and equilibrium constants. A previous theoretical study [Janin, J. & Wodak, S. J. (1985) Biopolymers 24, 509-526], using a highly simplified energy function, suggests that the R-like transition state is the result of a reaction pathway with the maximum buried surface area between alpha-beta-dimers.

引用

页码：4472 / 4475

页数：4

共 38 条

[1] ENERGETICS OF SUBUNIT ASSEMBLY AND LIGAND-BINDING IN HUMAN-HEMOGLOBIN [J].