Proteins are involved in almost all biological processes, and their function depends primarily on the correct three-dimensional folding of the polypeptide chain. However, the native structure 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 and their non-specific aggregation. Thus, to achieve proper folding and functionality, not only the correct amino acid sequence, but also an environment allowing folding and ensuring protein stability is required. To counteract these limitations, cells have evolved a machinery of molecular chaperones which supports folding often in an ATP dependent manner.

In our group, we focus on the characterization of spontaneous and chaperone-assisted protein folding and association with a broad spectrum of biophysical methods combined with in vivo approaches with a view to define molecular mechanisms.

We are currently engaged with exciting research in 3 different areas.

  • The 90 kDa heat shock protein (Hsp90) family & the 70 kDa heat shock protein (Hsp70) family
  • Small heat shock proteins (sHsps)
  • Antibody folding