Our young interdisciplinary research group focuses on the design of enzymes possessing different selectivities than seen in nature. For this we use state-of-the-art computational protein design software like Rosetta but also deep-learning based methods like ProteinMPNN and others to transfer active sites of known enzymes into a new environment - a different protein scaffold. This enables us to alter for example stereoselectivity or substrate specificity.
The gained designs are ordered as synthetic genes, cloned and manipulated using techniques of molecular biology, produced in E. coli or yeast and purified using chromatographic methods.
We use analytical chromatography methods like HPLC and GC as well as spectroscopic screens using UV/Vis and fluorescence spectrophotometers to detect the desired activities. We are going to use fluorescence-activated-cell sorting (FACS) to screen libraries and evolve the designs further. The structures of the gained enzymes will be solved using x-ray crystallography.
Additionally, we have cooperations with other groups using computational methods to design binders for small molecules as well as to (re)design enzymes for various reactions.
We are part of the Institute of Biochemistry at the Graz University of Technology, the initiative Integrative Structural Biology and Biophysics and within the framework of BioTechMed Graz.
