Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins.

@article{Viitanen1992PurifiedC6,
  title={Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins.},
  author={P. V. Viitanen and Anthony A. Gatenby and George H Lorimer},
  journal={Protein science : a publication of the Protein Society},
  year={1992},
  volume={1 3},
  pages={
          363-9
        }
}
In vitro experiments employing the soluble proteins from Escherichia coli reveal that about half of them, in their unfolded or partially folded states, but not in their native states, can form stable binary complexes with chaperonin 60 (groEL). These complexes can be isolated by gel filtration chromatography and are efficiently discharged upon the addition of Mg.ATP. Binary complex formation is substantially reduced if chaperonin 60 is presaturated with Rubisco-I, the folding intermediate of… CONTINUE READING

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