Molecular chaperones

摘要

Molecular chaperones were originally defined as a group of unrelated classes of proteins that mediate the correct assembly of other proteins, but are not by themselves components of the final functional structures. Chaperones can bind other proteins and by this virtue are able to stabilize otherwise unstable protein conformations, to control proteins release or their transport to a particular subcellular compartment, to promote proper protein folding and oligomeric assembly and to facilitate proteins disposal by degradation(Hartl, 1996; Hendrick and Hartl, 1993; Ranson et al.,1998).