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In biology, chaperones are peculiar proteins whose function is to assist other proteins in achieving proper folding. They have been discovered in being heat shock proteins[?], that is, proteins expressed in heat shock conditions. The reason for this behaviour is that protein folding is severly affected by heat, and therefore chaperones act to counteract the potential damage. Although most proteins can fold in absence of chaperones, a minority strictly requires them.

A large number of chaperones need ATP for proper function. However, chaperones are quite diverse and there is still considerable debate and uncertainity on how do they function.

Chaperones recognize unfolded proteins by the hydrophobic residues these expose to the solvent. This is an unnatural condition for properly folded proteins, that should expose hydrophilic aminoacids[?] only.

In former times, a chaperone was an older woman who accompanied a young unmarried woman on social occasions, especially when there were men present. Today, the term is used, often in a humorous manner, for anyone who accompanies a group of young people, especially in order to make sure that they behave properly.

In literature, probably the best known example of a plot revolving around the need for, and lack of, a chaperone is Brandon Thomas's farce Charley's Aunt[?] (1892).

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... the time of Justinian, he was a Christian and possibly bishop of Croton. In approximately 580, he wrote "De origine actibusque Getarum[?]" (The origin and deeds of the ...

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