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Molecular chaperones are ATP-consuming biological machines, which facilitatethe folding of proteins and RNA molecules that are kinetically trapped inmisfolded states for long times. Unassisted folding occurs by the kineticpartitioning mechanism according to which folding to the native state, with lowprobability as well as misfolding to one of the many metastable states, withhigh probability, occur rapidly on similar time scales. GroEL is an all-purposestochastic machine that assists misfolded substrate proteins (SPs) to fold. TheRNA chaperones (CYT-19) help the folding of ribozymes that readily misfold.GroEL does not interact with the folded proteins but CYT-19 disrupts both thefolded and misfolded ribozymes. Despite this major difference, the IterativeAnnealing Mechanism (IAM) quantitatively explains all the availableexperimental data for assisted folding of proteins and ribozymes. Driven by ATPbinding and hydrolysis and GroES binding, GroEL undergoes a catalytic cycleduring which it samples three allosteric states, referred to as T (apo), R (ATPbound), and R'' (ADP bound). In accord with the IAM predictions, analyses ofthe experimental data shows that the efficiency of the GroEL-GroES machineryand mutants is determined by the resetting rate $k_{R''\rightarrow T}$, whichis largest for the wild type GroEL. Generalized IAM accurately predicts thefolding kinetics of Tetrahymena ribozyme and its variants. Chaperones maximizethe product of the folding rate and the steady state native state fold bydriving the substrates out of equilibrium. Neither the absolute yield nor thefolding rate is optimized.

Iterative Annealing Mechanism Explains the Functions of the GroEL and RNA Chaperones