My scientific background is molecular structural biology and my main research interests concern the catalytic mechanism of enzymes at a molecular level and the structural determinants of enzyme function. To that end, I employ experimental techniques (e.g. biomolecular X-ray crystallography), but put special emphasis on the application of a whole repertoire of computational methods (e.g. homology modeling, docking, molecular dynamics simulations, calculation of the electrostatics within a protein,…).
I aim at understanding important enzyme characteristics such as substrate specificity, enantioselectivity, solubility or stability, and at exploiting this knowledge to rationally design enzyme mutants with tailor-made properties.
I have been working successfully in the field of structural enzymology for the past eight years and am currently involved in studies on coenzyme B12-dependent enzymes, on a number of enzymes utilized in industrial biocatalysis as well as on enzymic components of human lipid metabolism. Recently, I extended my research to the field of structural bioinformatics, where I focus on the analysis of protein-protein interactions in crystals and the identification of structural patterns which allow the prediction of enzyme function from structure.