调节严重急性呼吸综合征冠状病毒2型主要蛋白酶中的质子转移热力学：对催化作用和抑制剂设计的影响
Tuning Proton Transfer Thermodynamics in SARS-Cov-2 Main Protease: Implications for Catalysis and Inhibitor Design.
作者信息
Zanetti-Polzi Laura, Smith Micholas Dean, Chipot Chris, Gumbart James C, Lynch Diane L, Pavlova Anna, Smith Jeremy C, Daidone Isabella
机构信息
Center S3, CNR Institute of Nanoscience, Via Campi 213/A, I-41125 Modena, Italy.
Department of Biochemistry, Molecular and Cellular Biology, The University of Tennessee, Knoxville. 309 Ken and Blaire Mossman Bldg. 1311 Cumberland Avenue, Knoxville, TN 37996, United States.
出版信息
ChemRxiv. 2020 Nov 6:13200227. doi: 10.26434/chemrxiv.13200227.v1.
In this comutational work a hybrid quantum mechanics/molecular mechanics approach, the MD-PMM approach, is used to investigate the proton transfer reaction the activates the catalytic activity of SARS-CoV-2 main protease. The proton transfer thermodynamics is investigated for the apo ensyme (i.e., without any bound substrate or inhibitor) and in the presence of a inhibitor, N3, which was previously shown to covalently bind SARS-CoV-2 main protease.
在这项计算工作中，采用了一种混合量子力学/分子力学方法，即MD-PMM方法，来研究激活SARS-CoV-2主要蛋白酶催化活性的质子转移反应。研究了无辅基酶（即没有任何结合底物或抑制剂）以及存在抑制剂N3时的质子转移热力学，N3此前已被证明能与SARS-CoV-2主要蛋白酶共价结合。
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