Local unfolding of the HSP27 monomer regulates chaperone activity
The small heat-shock protein HSP27 occurs predominantly in oligomeric forms, which makes its structural characterisation challenging. Here the authors employ CPMG and high-pressure NMR with native mass spectrometry and biophysical assays to show that the active monomeric form of HSP27 is substantial...
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| Auteurs principaux: | , , , , , , , , |
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| Format: | article |
| Langue: | EN |
| Publié: |
Nature Portfolio
2019
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| Accès en ligne: | https://doaj.org/article/550a85efe9614ed0b28d5ac8d6498385 |
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