Getting newly synthesized proteins into shape

Abstract

Recent progress made in the analysis of in vivo folding of cytosolic proteins suggests that folding of cytosolic proteins occurs via multiple chaperone-assisted, as well as unassisted pathways. In the case of individual proteins, certain pathways may be highly favored. But, the cellular folding machinery also shows significant redundancy and flexibility, resulting in a variable network of folding pathways having alternative routes and backup systems.