Prof. Johannes Buchner
Mechanisms of Protein Folding
Proteins are involved in almost all biological processes, and their function depends primarily on the correct three-dimensional folding of the polypeptide chain. However, these structures must be dynamic and flexible, to exercise their biological function. As a result, the intrinsic stability of proteins is usually low. As the protein concentration in the cell is very high, this can lead to the interaction of partially folded proteins enhancing their non-specific aggregation. To counteract these limitations, cells have evolved a machinery of molecular chaperones which supports the folding of proteins. We aim for the characterization of spontaneous and chaperone-assisted protein folding and association with a view to define molecular mechanisms and biotechnological applications.
We are engaged in 3 major research areas.
- Analysis of the heat shock protein 90 and 70 (Hsp90, Hsp70) family
- Small heat shock proteins (sHsps)
- Antibodies as bio-therapeutics and antibody-based diseases (AL).