Protein folding is required for the realization of genetic information at the level of functional proteins and as such is one of the most fundamental reactions in all of biology. The Department is investigating the mechanisms of protein folding in the cell. Our long-term goal is to reach a complete understanding, at the structural and functional level, of how the machinery of molecular chaperones assists in co- and post-translational protein folding. Of special interest are the folding pathways in the cytosol of prokaryotes and eukaryotes. Using a range of methods from biophysics to cell biology, we ultimately seek to decipher the rules by which the thousands of different proteins in the cytosol utilize the chaperone machinery for de novo folding and assembly.
A second focus of research concerns the molecular mechanisms underlying neurodegenerative disorders, such as the polyglutamine diseases and Parkinson's disease, which are caused by aberrant protein folding and are associated with the formation of protein aggregates. Here we wish to understand how protein misfolding causes cytotoxicity and how molecular chaperones act as protective modulators. We plan to harness the power of the chaperone machinery for applications in biotechnological protein production and in combating disease