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Journal article

C-terminal interactions mediate the quaternary dynamics of αB-crystallin.

Abstract:

αB-crystallin is a highly dynamic, polydisperse small heat-shock protein that can form oligomers ranging in mass from 200 to 800 kDa. Here we use a multifaceted mass spectrometry approach to assess the role of the C-terminal tail in the self-assembly of αB-crystallin. Titration experiments allow us to monitor the binding of peptides representing the C-terminus to the αB-crystallin core domain, and observe individual affinities to both monomeric and dimeric forms. Notably, we find that binding...

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Publication status:
Published

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Publisher copy:
10.1098/rstb.2011.0405

Authors


Hilton, GR More by this author
Hochberg, GK More by this author
Laganowsky, A More by this author
McGinnigle, SI More by this author
Baldwin, AJ More by this author
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Journal:
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
Volume:
368
Issue:
1617
Pages:
20110405
Publication date:
2013-05-05
DOI:
EISSN:
1471-2970
ISSN:
0962-8436
URN:
uuid:85ec64f9-e559-4159-9182-79e909658a7d
Source identifiers:
390860
Local pid:
pubs:390860

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