My primary research interests are designing and engineering biomolecular structures and their functions – a strongly collaborative effort that combines structural biology, computational biology, biochemistry, biophysics approaches and bioorganic chemistry. I always was fascinated by structures of biological macromolecules and their relationship to function and therefore conducted my graduate work in protein crystallography and biocatalysis at the University of Graz, Austria. During this time I discovered a set of rules based on sequence-structure relationships that can now be used to inform industrial biotransformation reactions. In addition, I worked on deciphering the biosynthetic pathway of the antibiotic Nikkomycin, for which I did extensive computational modeling and solved the structure of a key-enzyme within the pathway.
To further expand my skill set, I joined the Baker Lab and subsequently was awarded a Marie Curie International Outgoing Fellowship to conduct my research here. Since I joined the lab, I, together with two co-workers, developed a method to parametrically design alpha-helical proteins. All the proteins we designed so far exhibited unprecedented stabilities. I’m currently working on broadening the approach and expanding the repertoire of designed structures to ones that don’t occur in nature. My future research aims are specifically directed towards the use of these highly stable designed protein structures to utilize them as building blocks for the design of higher complexity structures and biomaterials. I am specifically interested in building de-novo proteins that exhibit a pore for the potential use as molecular anchors/filters or for nanopore sequencing. Ultimately, I see my research combining the de-novo and material designs to built elaborated reaction networks with atomic level accuracy, mimicking biosynthetic pathways, that can be used to synthesize complex chemical compounds, or to build protein-matrices that can aid in tissue regeneration/engineering.