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线性自由能关系在蛋白质构象变化中的应用:血红蛋白的四级结构变化

Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

作者信息

Eaton W A, Henry E R, Hofrichter J

机构信息

Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.

出版信息

Proc Natl Acad Sci U S A. 1991 May 15;88(10):4472-5. doi: 10.1073/pnas.88.10.4472.

DOI:10.1073/pnas.88.10.4472
PMID:2034685
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC51682/
Abstract

The transition state for the R in equilibrium with 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.

摘要

与血红蛋白四级构象变化的T处于平衡状态的R的过渡态,其热力学性质与R构象的热力学性质更为接近,而与T构象的热力学性质相差较大。这一发现基于对活化和平衡焓变及熵变的比较,以及对四级反应速率和平衡常数之间线性自由能关系的观察。之前一项使用高度简化能量函数的理论研究[贾宁,J. & 沃达克,S. J.(1985年)《生物聚合物》24,509 - 526]表明,类R过渡态是αβ二聚体之间具有最大埋藏表面积的反应途径的结果。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d689/51682/743b829c9c21/pnas01060-0423-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d689/51682/743b829c9c21/pnas01060-0423-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d689/51682/743b829c9c21/pnas01060-0423-a.jpg

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