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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

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Publisher copy:
10.1073/pnas.0910126107

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Journal:
Proceedings of the National Academy of Sciences of the United States of America More from this journal
Volume:
107
Issue:
5
Pages:
2007-2012
Publication date:
2010-02-01
DOI:
EISSN:
1091-6490
ISSN:
0027-8424

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