ATP与多亚基酶结合的统计热力学分析
ATP binding to a multisubunit enzyme: statistical thermodynamics analysis
摘要：
由于亚基间的通讯，多亚基酶通常以协同的方式水解ATP。然而，到目前为止，人们对这一过程的原理仍知之甚少。在这项研究中，从统计热力学的观点，一个简单的模型。在这个模型中，我们假设ATP的结合会改变相应酶亚基的电势，而这种改变的程度取决于其相邻亚基的状态。酶在给定状态下的概率满足玻尔兹曼分布。虽然该模型看起来很简单，但它能很好地拟合伴侣蛋白TRiC/CCT的最新实验数据。从该模型可以得到TRiC/CCT的主导态。该研究为利用统计热力学分析来理解生物物理过程提供了一条新的途径。
英文摘要：
Due to inter-subunit communication, multisubunit enzymes usually hydrolyze ATP in a concerted fashion. However, so far the principle of this process remains poorly understood. In this study, from the viewpoint of statistical thermodynamics, a simple model is presented. In this model, we assume that the binding of ATP will change the potential of the corresponding enzyme subunit, and the degree of this change depends on the state of its adjacent subunits. The probability of enzyme in a given state satisfies the Boltzmann's distribution. Although it looks much simple, this model can fit the recent experimental data of chaperonin TRiC/CCT well. From this model, the dominant state of TRiC/CCT can be obtained. This study provided a new way to understand biophysical processes by statistical thermodynamics analysis.
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