Nature, Vol.381, No.6583, 571-580, 1996
Molecular Chaperones in Cellular Protein-Folding
The folding of many newly synthesized proteins in the cell depends on a set of conserved proteins known as molecular chaperones. These prevent the formation of misfolded protein structures, both under normal conditions and when cells are exposed to stresses such as high temperature. Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.
Keywords:HEAT-SHOCK PROTEINS;RIBULOSE BISPHOSPHATE CARBOXYLASE;ESCHERICHIA-COLI GROEL;ATP HYDROLYSIS;THERMOPHILIC ARCHAEBACTERIUM;BINDING-SPECIFICITY;CENTRAL CAVITY;TRANSLOCATION;COMPLEX;DNAK