Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds.

@article{Ranson1995ChaperoninsCC,
  title={Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds.},
  author={Neil A. Ranson and Nicholas J Dunster and Steven G. Burston and A. R. Clarke},
  journal={Journal of molecular biology},
  year={1995},
  volume={250 5},
  pages={581-6}
}
Chaperonins use energy derived from ATP hydrolysis to enhance the efficiency of protein folding by a mechanism which remains a matter of debate. Here, we show that the kinetics of spontaneous and assisted folding of mitochondrial malate dehydrogenase are quantitatively described by a simple physical model. The protein folds from non-native chains by the slow formation of native-like monomers, which then dimerize to form the active enzyme. Misfolding proceeds by two phases of aggregation: the… CONTINUE READING

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