GroEL–Substrate Interactions Molding the Fold, or Folding the Mold?

@article{Feltham2000GroELSubstrateIM,
  title={GroEL–Substrate Interactions Molding the Fold, or Folding the Mold?},
  author={Joanna L Feltham and Lila M. Gierasch},
  journal={Cell},
  year={2000},
  volume={100},
  pages={193-196}
}
(K d in the low micromolar range). As a first step, Chen and Sigler formed cocrystals of the SBP peptide and the isolated apical domain of GroEL (residues 191–336), and Molecular chaperones ensure that proteins achieve and solved this structure at high resolution (2.1 A ˚ , see Figure maintain their proper folds in the appropriate cellular 2a). They have also solved and partially refined a struc-compartments. Among this fascinating class of biologi-ture of the SBP peptide complexed with the… CONTINUE READING
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to reconcile straightforwardly with binding to any pre(

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