Our research is focused on molecular structural biology and our main interests concern the catalytic mechanism of enzymes at a molecular level and the structural determinants of enzyme properties. To that end, we employ experimental techniques (mainly biomolecular X-ray crystallography), but put special emphasis on the application of a whole repertoire of computational methods (such as homology modeling, docking, molecular dynamics simulations, calculation of the electrostatics within a protein,…). We aim at understanding important enzyme characteristics and at exploiting this knowledge to rationally design enzyme mutants with tailor-made properties. In the field of structural bioinformatics we study protein-protein interactions in crystals and try to identification of structural patterns in enzyme active sites which allow the prediction of enzyme function from structure.
Monika Oberer's team aims to understand the function of proteins on the molecular level. Knowledge of the three-dimensional structures of proteins is an essential prerequisite for achieving this aim. The results of our research are always seen in the biological context, since proteins do not function as isolated molecules . A long-term goal of our group is to establish structure-function relationships of proteins in intracellular and intravascular lipid metabolism. The proteins under investigation are key molecules in numerous biological processes. They also control the accessibility of lipids to produce energy. Furthermore, organisms use lipids and their metabolic products as building blocks for the synthesis of new molecules or for signal transduction. Dysregulation of metabolic proteins leads to various pathological conditions, including cardiovascular diseases, type 2 diabetes and various lipid metabolism disorders. In our laboratory, we determine protein structures using X-ray crystallography and NMR spectroscopy. In addition, we employ further biochemical and biophysical methods to characterize the proteins and the corresponding interactions.
Life itself depends on the interactions of biomolecules, which are three-dimensional, flexible objects. My research focuses on understanding their behaviours. In my group, we study the structural, functional, dynamic and thermodynamic properties of biological systems using computational methods such as structural bioinformatics, data mining and artificial intelligence. We employ various incarnations of the "Catalophore" approach, a method describing the multivariate, volumetric property-fields projected by biomolecules into their environment. These property fields are, in principle, independent of the underlying biomolecular structure, allowing analysis beyond sequence and structure. Combined with modern high-performance computing techniques, this enables a deeper understanding of biological processes and contributes to future drug and protein research applications.