Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.

@article{Farr2007PerturbedAA,
  title={Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.},
  author={George W. Farr and Wayne Fenton and Arthur L Horwich},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 13},
  pages={5342-7}
}
Folding of substrate proteins inside the sequestered and hydrophilic GroEL-GroES cis cavity favors production of the native state. Recent studies of GroEL molecules containing volume-occupying multiplications of the flexible C-terminal tail segments have been interpreted to indicate that close confinement of substrate proteins in the cavity optimizes the rate of folding: the rate of folding of a larger protein, Rubisco (51 kDa), was compromised by multiplication, whereas that of a smaller… CONTINUE READING
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