Local unfolding of the HSP27 monomer regulates chaperone activity
oleh: T. Reid Alderson, Julien Roche, Heidi Y. Gastall, David M. Dias, Iva Pritišanac, Jinfa Ying, Ad Bax, Justin L. P. Benesch, Andrew J. Baldwin
| Format: | Article |
|---|---|
| Diterbitkan: | Nature Portfolio 2019-03-01 |
Deskripsi
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 substantially disordered and highly chaperone-active.