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Molecular chaperones: providing a safe place to weather a midlife protein-folding crisis

Nature Structural & Molecular Biology volume 23, pages 621623 (2016) | Download Citation

Contrary to conventional wisdom that molecular chaperones rely on hydrophobic interactions to bind a wide variety of client proteins in danger of misfolding, three recent studies reveal that the ATP-independent chaperone Spy exploits electrostatic interactions to bind its clients quickly, yet loosely enough to enable folding of the client while it is chaperone bound.

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Author information

Affiliations

  1. Patricia L. Clark is at the Department of Chemistry & Biochemistry and the Department of Chemical & Biomolecular Engineering, Eck Institute for Global Health, University of Notre Dame, Notre Dame, Indiana, USA.

    • Patricia L Clark
  2. Adrian H. Elcock is at the Department of Biochemistry, University of Iowa, Iowa City, Iowa, USA.

    • Adrian H Elcock

Authors

  1. Search for Patricia L Clark in:

  2. Search for Adrian H Elcock in:

Competing interests

The authors declare no competing financial interests.

Corresponding author

Correspondence to Patricia L Clark.

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DOI

https://doi.org/10.1038/nsmb.3255

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