An important part of our research focuses on studying the evolution of proteins and enzymes in traits such as enzymatic promiscuity, substrate specificity, allosteric regulation, catalytic mechanisms, and adaptation to various extreme environments (psychrophiles, thermophiles, halophiles).

We employ the methodology of ancestral enzyme reconstruction to trace the evolutionary pathways of these traits and the associated structural aspects. In addition to X-ray crystallography, SAXS, and cryoEM, we utilize approaches such as steady-state enzymatic kinetics, rapid kinetics (pre-steady-state), fluorescence, circular dichroism, thermodynamic studies of molecular interactions, protein stability, bioinformatics, computational molecular dynamics simulations, and recently, multiparametric single-molecule fluorescence.