Computational (bio)chemistry has become an integral part of our understanding of chemical and biological systems and processes. Specifically, it has greatly assisted in shedding light on the catalytic action of metalloproteins, mostly by elucidating their reaction mechanisms. The accumulated expertise, applicability of modern quantum mechanical methods for realistic systems, availability of reasonably accurate solvation models and QM/MM-like coupling schemes along with bioinformatics or structural search engines may ultimately unleash its predictive power and lead to a delivery of a material output in near future.
Major efforts of the group aim at an ab initio design of both small catalytic metallopeptides and highly specific metal chelators. Our approach involves development of a unique set of computer programs operating on top of a database of peptidic fragments obtained from the Protein Data Bank or resulting from large-scale conformational searches of short peptides and merging them into a predefined (single-chain) scaffold, either mimicking a protein active site or a chelator. A sophisticated coupling to external QM or QM/MM(MD) programs is implemented to verify inherent stability and catalytic properties of the designed systems.
Other research topics in the group include development of quantum and molecular mechanical (QM/MM) methods, organic reactivity, computational homogeneous catalysis, protein-ligand interactions, computational electrochemistry, theoretical spectroscopy, relativistic quantum chemistry, and design of novel fullerenes that can act as molecular switches, transistors, and memristors. Our recent contributions to general chemical knowledge include theoretical and experimental proof of hydrogen bonding to gold or to understanding of heavy-atom effects on NMR chemical shifts across the periodic table.