High selectivity with low specificity: how SecB has solved the paradox of chaperone binding.

@article{Randall1995HighSW,
  title={High selectivity with low specificity: how SecB has solved the paradox of chaperone binding.},
  author={Linda L Randall and Stephen John Hardy},
  journal={Trends in biochemical sciences},
  year={1995},
  volume={20 2},
  pages={65-9}
}
Fundamental to the function of all molecular chaperones is their amazing ability to selectively and rapidly bind proteins in non-native states. Chaperones modulate a kinetic partitioning among the alternative pathways open to polypeptides within a cell, so that the proper pathway is taken. Here we review studies of SecB, a chaperone in Escherichia coli dedicated to facilitation of protein export, and emphasize the features that enable it to bind rapidly with high affinity and selectivity in the… CONTINUE READING

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