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...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2019-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-019-08557-8 |