Analysis of the physical nature of catalytic effects: Development and applications of bottom-up methods for/ab initio/ catalyst inverse design/via/ catalytic fields

Catalytic or inhibitory effects in proteins are governed by  intermolecular interactions. Analysis of the hierarchy of approximate theoretical models based on  well defined physical components permitted us to derive new nonempirical methods capable to determine key effects responsible for catalytic [1] activity. The dominant electrostatic nature of catalytic activity in enzymes  allowed us to derive static and dynamic catalytic fields, which have been used to predict mutation [2] or substitution [3] effects, explain extreme catalytic activity of  enzyme involving strong hydrogen bond chains [4] or to verify alternative reaction  mechanisms in enzymes [5].

Acknowledgments: NCN OPUS grant 2017/27/B/ST4/01327 „Catalytic fields as  the tool for theoretical analysis and design of biocatalysts"

Literature:
[1] W. Beker, W.A. Sokalski, J.Chem.Theor.Comp., 16 (2020) 3420-3429.
[2] W. Beker, M. van der Kamp, A. Mulholland, W.A. Sokalski,  J.Chem.Theor.Comp., 13(2017)945-955.
[3] M. Chojnacka, M. Feliks, W. Beker,W.A. Sokalski, J.Mol.Model., 24  (2018) 28.
[4] P. Kędzierski, M. Zaczkowska, W.A. Sokalski, J.Phys.Chem.B, 124  (2020)3661-3666.
[5] P. Kedzierski, M. Moskal, W. A. Sokalski, J.Phys.Chem.B, 125  (2021)11606-11616.