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

Nature Structural & Molecular Biology volume 23, pages 621–623 (2016)Cite this article

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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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Figure 1: Protein folding involves the selective stabilization of the functional native conformation (N) of a protein, versus globally unfolded conformations (U), partially folded intermediates (I) and misfolded states (A).
Figure 2: Effects of Spy binding on the folding-energy landscape of Im7, a model in vivo substrate.

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Authors and 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

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  1. Patricia L Clark
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  2. Adrian H Elcock
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Correspondence to Patricia L Clark.

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Clark, P., Elcock, A. Molecular chaperones: providing a safe place to weather a midlife protein-folding crisis. Nat Struct Mol Biol 23, 621–623 (2016). https://doi.org/10.1038/nsmb.3255

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