The main objective of research is to understand the structural basis of metalloprotein functions, with particular interest in iron and copper-containing enzymes. The proteins are purified from various organisms, the corresponding genes identified, cloned, sequenced, and the proteins finally heterologously overexpressed (Escherichia coli, Pichia pastoris, Chinese hamster ovary-, HEK-cell lines).
Exchange of amino acids by either site-directed or random mutagenesis in combination with biophysical methods (electron paramagnetic resonance spectroscopy, resonance Raman spectroscopy, UV-Vis- and fluorescence spectroscopy, circular dichroism spectroscopy, differential scanning calorimetry), transient- and steady-state kinetic investigations (multi-mixing stopped-flow spectroscopy) and X-ray crystallography allow elucidation of structure and function including detailed characterization of the corresponding redox intermediates, which are relevant in catalysis. In addition we ask for the role of post-translational modifications in the prosthetic groups and the protein matrix in catalysis of oxidoreductases.
We also prepare (recombinant) enzymes for customers (http://www.myeloperoxidase.com/) and provide quality control and kinetic analyses of (recombinant) proteins.
In a recently started Christian Doppler Laboratory for Antibody Engineering (2009-2016) new generations of engineered monoclonal antibodies with improved properties are being developed. We aim to design stable antibodies and antibody fragments of extended lifespan and additional binding sites by engineering both the protein scaffold and the non-CDR loops of constant or variable domains.
Furthermore the group coordinates the the Doctoral Program-plus Biomolecular Technology of Proteins – BioToP (2010-2022).