Protein unfolding as a switch from self-recognition to high-affinity client binding
Under stress conditions the molecular chaperone Hsp33 is activated to process unfolded proteins. Here, the authors use in vivo and in vitro crosslinking and 19F-NMR to elucidate the binding site for misfolded proteins and are able to propose a model for its mechanism of action.
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| Auteurs principaux: | , , , , , , , |
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| Format: | article |
| Langue: | EN |
| Publié: |
Nature Portfolio
2016
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| Sujets: | |
| Accès en ligne: | https://doaj.org/article/695b2905d3a942f196334c70c8cf5b8c |
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