【摘要】 分子力学泊松-玻尔兹曼溶剂可及表面积(MM/PBSA)是一种非常主流的计算生物大分子体系结合自由能的方法,但是其中熵变的计算一直以来都是理论计算上的难点.2016年发展的相互作用熵方法因其理论严谨、计算成本低等优势得到了广泛的应用.该方法已在周期蛋白依赖性激酶2、胰蛋白酶、HIV蛋白酶、间变性淋巴瘤激酶与配体以及P53与MDMX/MDM2等一些关键的体系上得到了应用,这为研究者理解生物大分子中相互作用的机理提供了可信且新颖的途径.本文介绍了相互作用熵方法的发展,并为其在生物大分子中的应用提供了可行的指引和建议.更多还原

【Abstract】 The molecular mechanics/Poisson-Boltzmann solvent surface area is a very popular method for predicting the binding free energy of bio-macromolecule systems, while the calculation of entropy change is suffering the developmental bottleneck. The proposed interaction entropy method in 2016 has been widely used in the prediction of entropic contribution, due to its rigorous theory, low computational cost and high accuracy. This approach has provided a credible and novel approach for researchers to understand the mechanisms of interactions in biological macromolecules, such as CDK2, HIV protease, ALK, MDMX/MDM2 and so on. This review is intended to introduce the development of interaction entropy method, and provides practical guidance and advice for its application in bio-macromolecules.更多还原