Fig. 1.

The general chaperone cycle of Heat shock proteins. Initially, unfolded client protein bound to the HSP70-HSP40 chaperones interacts with the HSP90. ATP binding to HSP90 induces the client proteins transfer from HSP70 to HSP90. Later, the conformation of HSP70-HSP40 chaperones will be released. Finally, the hydrolysis of ATP induces additional conformation changes leading to the client protein release