Ułatwienia dostępu
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.