THE EFFECT OF MOLECULAR CHAPERONES ON IN-VIVO AND IN-VITRO FOLDING PROCESSES

Numerous successful experiments of in vitro protein folding demonstrat e that all information required for the formation of the native, three -dimensional structure of a protein is encoded in the amino acid seque nce. Thus, in vivo folding was long considered an autonomous process u naffected by other proteins or cellular components. This central parad igm of in vivo protein structure formation was abandoned with the iden tification of molecular chaperones which facilitate protein folding bo th in vitro and in vivo. Recently, mechanistic details of chaperone ac tion have been analyzed at a molecular level. Members of the molecular chaperone families seem to fulfil different tasks along the folding p athway. Understanding the mechanism of the chaperone machinery will he lp to design efficient folding processes for the in vitro folding of m isfolded recombinant proteins. Furthermore, cellular fine-tuning of th e chaperone machinery may provide new tools for the prevention of misf olding of recombinant proteins.