Chaperones, chaperonins and heat-shock proteins

The protein folding of a nascent polypeptide is the decoding of the linear information contained in the primary sequence into the native and functionally active three-dimensional conformation. Chaperone proteins and folding catalysts may contribute to successful folding into the native and active protein conformation in the crowded cellular environment, thus avoiding aggregation of non-native protein forms. Molecular chaperones in vivo play a pivotal role in the maintenance of the proteome quality control and in the correct balance between protein folding and degradation. The unbalance of the equilibrium between protein synthesis, protein folding and protein degradation may contribute to protein misfolding and aggregation which may lead to the onset of several degenerative diseases associated with protein aggregation, such as Alzheimer’s and Huntington’s disease.