Protein Folding and Chaperones
Published Online: 17 JUN 2010
Copyright © 2001 John Wiley & Sons, Ltd. All rights reserved.
How to Cite
Sinnige, T., Karagöz, G. E. and Rüdiger, S. G. 2010. Protein Folding and Chaperones. eLS. .
- Published Online: 17 JUN 2010
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Proteins fold via specific pathways to achieve their native structure. Protein structures are, however, inherently unstable; hence folding and unfolding are in equilibrium. Protein instability is a major concern inside the cell. Specialised proteins called molecular chaperones are, therefore, required to assist proteins in folding and to prevent aggregation of folding intermediates. Many different classes of chaperones exist that are conserved throughout all kingdoms of life, many of which are known as heat-shock proteins. Chaperones typically recognise hydrophobic patches, but the exact functions and mechanisms of action of the various chaperone classes are very different. The main chaperone classes Hsp70, Hsp90, Hsp100 and chaperonins all depend on adenosine triphosphatase (ATPase) cycles, which enable subtle activity control by co-chaperones. The molecular understanding of the mechanism of both chaperones and protein folding are key problems in today's life sciences. The importance is illustrated by the fact that many diseases are associated with these processes.
Proteins fold via pathways.
Protein structures are labile.
Protein folding in vivo is assisted by molecular chaperones.
Assisted protein folding requires ATP energy.
Molecular chaperones are evolutionarily conserved.
Chaperone activity is controlled by co-chaperones and cofactors.
Chaperone families differ in structure and function.
- protein folding;
- protein stability;
- molecular chaperones;
- folding pathways;
- heat-shock response;
- protein misfolding;
- intrinsically disordered proteins