Chaperones and protein folding: an introduction

The activity of most proteins is linked to specific structure. Protein structures are usually characterized by a hydrophobic core and a hydrophilic surface. Much less is known about the properties of protein structures during protein folding and unfolding processes. Protein folding problems are a central topic in cell biology and medicine. Diseases that are linked to protein folding include cancer and amyloid diseases such as Creutzfeld-Jakob and Alzheimer.

Unfolded proteins are difficult to study because of their heterogeneous nature and their tendency to aggregate. They are the substrates of molecular chaperones, which inside the cell take care of proteins that are not fully folded. Studying chaperone complexes allows bicochemical access to these otherwise mysterious species. Hsp90 chaperones constitute a particular exiting chaperone class. They are evolutionary conserved, appear in most compartments and most substrates are oncogenes. The main direction of our research is to understand protein folding in the cell via studying Hsp90.

• CHAPERONE DUTIES IN THE CELL
  Most proteins require a specific three dimensional conformation to be functional active. Folding and unfolding processes in the cell are controlled by molecular chaperones (green arrows, folding processes; red arrows, chaperone action).

For a broader introduction to chaperones and protein folding go to the Department's research overview pages

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