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Quaternary dynamics and plasticity underlie small heat shock protein chaperone function

Abstract:

Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that prevent protein aggregation by binding clients destabilized during cellular stress. Here we probe the architecture and dynamics of complexes formed between an oligomeric sHSP and client by employing unique mass spectrometry strategies. We observe over 300 different stoichiometries of interaction, demonstrating that an ensemble of structures underlies the protection these chaperones confer to unfolding clients....

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

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Publisher copy:
10.1073/pnas.0910126107

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Department:
Pembroke College
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Department:
Exeter College
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Department:
University College
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Publisher:
National Academy of Sciences Publisher's website
Journal:
Proceedings of the National Academy of Sciences of the United States of America Journal website
Volume:
107
Issue:
5
Pages:
2007-2012
Publication date:
2010-02-25
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
Pubs id:
pubs:59335
URN:
uri:80bc4bde-76f2-49e0-bbef-bbb9dfc2e1c0
UUID:
uuid:80bc4bde-76f2-49e0-bbef-bbb9dfc2e1c0
Local pid:
pubs:59335
Language:
English
Keywords:

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