血红蛋白协同作用的结构特异性模型。
Structure-specific model of hemoglobin cooperativity.
作者信息
Lee A W, Karplus M
出版信息
Proc Natl Acad Sci U S A. 1983 Dec;80(23):7055-9. doi: 10.1073/pnas.80.23.7055.
Abstract
A generalization of the Szabo-Karplus statistical mechanical model for hemoglobin cooperativity is formulated. The model fits the available thermodynamic and spectroscopic data with assumptions that are consistent with structural results and empirical energy function calculations. It provides a mechanism of hemoglobin cooperativity that is a generalization of the proposals of Monod, Wyman, and Changeux and of Perutz. The role of nonsalt-bridge related sources of constraints on ligand affinity and the mode of salt-bridge coupling to tertiary-quaternary structural changes are examined within the framework of the model. Analysis of proton release data for a range of pH values indicates that a pH-independent part of cooperativity must be present. The pH dependence of the first and last Adair constants point to partial linkage of salt bridges to ligation in the deoxy state and to a destabilized intra-beta-chain salt bridge in the unliganded oxy state.
摘要
提出了一种对血红蛋白协同性的萨博 - 卡尔普拉斯统计力学模型的推广。该模型通过与结构结果和经验能量函数计算相一致的假设，拟合了现有的热力学和光谱数据。它提供了一种血红蛋白协同性机制，是对莫诺德、怀曼和尚热以及佩鲁茨提议的推广。在该模型框架内，研究了与盐桥无关的配体亲和力约束来源的作用以及盐桥与三级 - 四级结构变化的耦合模式。对一系列pH值下质子释放数据的分析表明，必须存在与pH无关的协同性部分。第一个和最后一个阿代尔常数的pH依赖性表明，在脱氧状态下盐桥与配体结合存在部分联系，而在未结合配体的氧合状态下，β链内盐桥不稳定。
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