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Heat-Shock Proteins

support the maintenance of three dimensional structures of proteins for instance by protecting them from denaturation due to heat. They can be found everywhere in the organism and are expressed extensively, for example, under stress condition caused by exposure to high heat, UV-rays or ethanol.

Many belong to the family of chaperons which play a role in protein translocation, and folding and assembly, also under standard conditions. Chaperons do not contain information about the protein specific three dimensional folding but generally accelerate and facilitate folding by inhibiting aggregation and defective bindings. are distinguished in categories according to their molecular weight.

The most researched heat-shock proteins are , and . The numerical value is the molecular weight in kilo Daltons. is an important component of the chaperon system in animal organisms. recognizes collapsed substrate proteins, which would aggregate otherwise, and folds them actively under consumption of ATP. on the other hand helps to maintain the unfolded condition of target proteins.

The chaperone family proteins are ubiquitous in prokaryotes and eukaryotes and apparently prevent the final steps of the protein folding process. interact with actin and tubulin and in concert with , as well as others, function as a supramolekular complex.

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