The Mechanism and Function of Group II Chaperonins.

@article{Lopez2015TheMA,
  title={The Mechanism and Function of Group II Chaperonins.},
  author={Tom Lopez and Kevin M. Dalton and Judith Frydman},
  journal={Journal of molecular biology},
  year={2015},
  volume={427 18},
  pages={2919-30}
}
Protein folding in the cell requires the assistance of enzymes collectively called chaperones. Among these, the chaperonins are 1-MDa ring-shaped oligomeric complexes that bind unfolded polypeptides and promote their folding within an isolated chamber in an ATP-dependent manner. Group II chaperonins, found in archaea and eukaryotes, contain a built-in lid that opens and closes over the central chamber. In eukaryotes, the chaperonin TRiC/CCT is hetero-oligomeric, consisting of two stacked rings… CONTINUE READING
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