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Evaluating the effect of phosphorylation on the structure and dynamics of Hsp27 dimers by means of ion mobility mass spectrometry

Abstract:

The quaternary structure and dynamics of the human small heat-shock protein Hsp27 are linked to its molecular chaperone function and influenced by post-translational modifications, including phosphorylation. Phosphorylation of Hsp27 promotes oligomer dissociation and can enhance chaperone activity. This study explored the impact of phosphorylation on the quaternary structure and dynamics of Hsp27. Using mutations that mimic phosphorylation, and ion mobility mass spectrometry, we show that suc...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted Manuscript

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Publisher copy:
10.1021/acs.analchem.7b03328

Authors


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ORCID:
0000-0001-7999-1385
Aquilina, JA More by this author
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Physical & Theoretical Chem
Oxford college:
University College
Publisher:
American Chemical Society Publisher's website
Journal:
Analytical Chemistry Journal website
Volume:
89
Issue:
24
Pages:
13275-13282
Publication date:
2017-11-14
Acceptance date:
2017-11-14
DOI:
EISSN:
1520-6882
ISSN:
0003-2700
Pubs id:
pubs:810114
URN:
uri:5772364e-5256-49c5-8664-c7972acf0e25
UUID:
uuid:5772364e-5256-49c5-8664-c7972acf0e25
Local pid:
pubs:810114

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