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Journal article

Local unfolding of the HSP27 monomer regulates chaperone activity

Abstract:

The small heat-shock protein HSP27 is a redox-sensitive molecular chaperone that is expressed throughout the human body. Here we describe redox-induced changes to the structure, dynamics, and function of HSP27 and its conserved α-crystallin domain (ACD), and provide the first structural characterization of a small heat-shock protein monomer using nuclear magnetic resonance (NMR) spectroscopy. While HSP27 assembles into oligomers, we show that the transiently populated monomers that are releas...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-019-08557-8

Authors


More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
10
Article number:
1068
Publication date:
2019-03-06
Acceptance date:
2019-01-05
DOI:
EISSN:
2041-1723
Keywords:
Pubs id:
pubs:965607
UUID:
uuid:d2a68ded-19e8-4498-97a2-85c01d542ed1
Local pid:
pubs:965607
Source identifiers:
965607
Deposit date:
2019-01-22

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