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Local unfolding of the HSP27 monomer regulates chaperone activity
- Source :
- Nature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
- Publication Year :
- 2019
- Publisher :
- Nature Portfolio, 2019.
-
Abstract
- 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.
- Subjects :
- Science
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 10
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Nature Communications
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.550a85efe9614ed0b28d5ac8d6498385
- Document Type :
- article
- Full Text :
- https://doi.org/10.1038/s41467-019-08557-8