Chaperones are proteins that play a role in the assembly or proper folding of other proteins without themselves being components of the later' They prevent faulty folding and unproductive interactions of other proteins. Properties of chaperones : Present in a wide range of species from bacteria to humans Many are so-called 'Heat shock proteins' (HSP) Some are inducible by conditions that cause unfolding or aggregation of proteins (e.g. Elevated temperature and various chemicals) They bind to predominantly hydrophobic regions of unfolded or aggregated proteins They act in part as a quality control or editing mechanism for detecting misfolded in the protein chaperone interaction Found in various cellular compartments such as cytosol, mitochondria and lumen of endoplasmic reticulum. About other optionsProteases are enzymes that hydrolyze proteins Proteosomes (e.g. 26S component) help in degrading the proteins marked with ubiquitin The template is involved in the synthesis of nucleic acids