“…As a result, GroEL/ES provides kinetic assistance to the folding process and accelerates the folding of various proteins ~ 20‐ to 100‐fold above their spontaneous folding rate. These include destabilized variants of maltose‐binding protein (MBP) [59,60,63–65], Rhodospirillum rubrum Rubisco [66,67], bacterial proteins with topological knots [68], the E. coli prolidase enzyme PepQ [62], and several E. coli proteins with a (βα)8 TIM‐barrel fold [55,61]. In all cases, the slower rate of spontaneous folding was not due to transient aggregation, implying that the chaperonin altered the folding energy landscape for these substrates.…”