Jochen Reinstein Group - Molecular Chaperones
Attaining a well defined three dimensional structure and thus functionality can be a serious challenge in the early life of many proteins. Although the final structure is energetically favored, many side reactions can occur mostly leading to aggregation that prevent the formation of the native protein structure.
Molecular chaperones are ubiquitous in prokarytic/eukaryotic organisms and form cellular networks which assist protein folding in the cell. The underlying mechanisms, often dependent on the chemical energy of ATP, are diverse and complex. The DnaK/Hsc70 system on its own is mainly involved in preventing aggregation of challenged protein substrates, but in cooperation with ClpB/Hsp104 it can also rescue already aggregated proteins.
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Protein Folding – chaperones help to prevent and revert unproductive pathways
Jochen Reinstein
The individual folding properties and potential recognition sequences of target proteins, raise the question about overall balance versus optimization of chaperon assisted folding.
