期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 27, 期 10, 页码 3407-3419出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.202003978
关键词
electron density; electrostatic potential; intermolecular interactions; polarization; protease inhibitor
资金
- German Research Foundation (DFG) via the Emmy-Noether project [GR 4451/1-1]
- Australian Research Council (ARC) [DP110105 347]
- German Academic Scholarship Foundation (Studienstiftung des Deutschen Volkes)
- Projekt DEAL
The study compared the crystal interaction density and the enzyme interaction density, finding them to be very similar but with noticeable consequences for derived properties.
The crystal interaction density is generally assumed to be a suitable measure of the polarization of a low-molecular weight ligand inside an enzyme, but this approximation has seldomly been tested and has never been quantified before. In this study, we compare the crystal interaction density and the interaction electrostatic potential for a model compound of loxistatin acid (E64c) with those inside cathepsin B, in solution, and in vacuum. We apply QM/MM calculations and experimental quantum crystallography to show that the crystal interaction density is indeed very similar to the enzyme interaction density. Less than 0.1 e are shifted between these two environments in total. However, this difference has non-negligible consequences for derived properties.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据