Zhou H X
Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong.
Biophys J. 1997 Nov;73(5):2441-5. doi: 10.1016/S0006-3495(97)78272-9.
Electrostatic interactions are known experimentally to enhance the rate of protein-protein association by three to four orders of magnitude. However, theoretical efforts to quantitatively account for such rate enhancement have been hampered by the need to consider a large number of relative configurations of two associating proteins sampled during their diffusional encounter. Our recent work indicates that a good estimate of the rate enhancement is given by the average Boltzmann factor in the region of configurational space where association can effectively take place. This estimate is tested on a model system consisting of two spherical proteins, each with a "reactive patch." Three different forms of interaction potential are considered. Comparison with exact results for the association rate constant demonstrates that predictions based on the local Boltzmann factor are accurate to within approximately 50% for realistic sizes of the reactive region and amplitudes of the interaction potential.
实验表明，静电相互作用可将蛋白质 - 蛋白质结合速率提高三到四个数量级。然而，由于需要考虑两个结合蛋白质在扩散相遇过程中采样的大量相对构型，定量解释这种速率增强的理论研究受到了阻碍。我们最近的工作表明，结合速率增强的一个良好估计值由构型空间中结合能够有效发生的区域内的平均玻尔兹曼因子给出。这个估计值在一个由两个球形蛋白质组成的模型系统上进行了测试，每个蛋白质都有一个“反应性补丁”。考虑了三种不同形式的相互作用势。与结合速率常数的精确结果比较表明，对于反应区域的实际大小和相互作用势的幅度，基于局部玻尔兹曼因子的预测精确到大约50%以内。
