Fig. 6 | Nature Communications

Fig. 6

From: Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium

Fig. 6

Comparison of ATPase and protein folding activity between Ch-CPN WT and the pivot joint mutant (L439A). Error bars are ± s.d. for triplicate experiments. a ATP hydrolysis rates of Ch-CPN compared with the L439A mutant. ATPase activities of Ch-CPN and the L439A mutant were determined after incubation for 5 min at the indicated temperature by using the malachite green assay. b Refolding of Malate Dehydrogenase (MDH) by Ch-CPN wild type and the L439A mutant. Denatured MDH was mixed with Ch-CPN and the L439A mutant at 42 °C, respectively. The specific activity of MDH prior to denaturation was the control used to determine 100%

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