APPLICATION OF LINEAR FREE-ENERGY RELATIONS TO PROTEIN CONFORMATIONAL-CHANGES - THE QUATERNARY STRUCTURAL-CHANGE OF HEMOGLOBIN
APPLICATION OF LINEAR FREE-ENERGY RELATIONS TO PROTEIN CONFORMATIONAL-CHANGES - THE QUATERNARY STRUCTURAL-CHANGE OF HEMOGLOBIN
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DOI：
10.1073/pnas.88.10.4472
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发表时间：
1991-05-01
影响因子：
11.1
通讯作者：
HOFRICHTER, J
中科院分区：
文献类型：
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作者：
EATON, WA;HENRY, ER;HOFRICHTER, J
血红蛋白的四个构象变化的过渡态的R箭头指向右，而不是指向左，其热力学性质更接近于R构象而不是T构象。这一发现是基于对激活和平衡焓和熵变化的比较，以及对四元速率和平衡常数之间的线性自由能关系的观察。先前的一项理论研究[Janin， J. & Wodak， S. J. (1985) Biopolymers 24, 509-526]，使用高度简化的能量函数，表明R-like过渡态是α - β -二聚体之间具有最大掩埋表面积的反应途径的结果。
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.