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Journal article

Proline isomerization in the C-terminal region of HSP27

Abstract:

In mammals, small heat-shock proteins (sHSPs) typically assemble into interconverting, polydisperse oligomers. The dynamic exchange of sHSP oligomers is regulated, at least in part, by molecular interactions between the α-crystallin domain and the C-terminal region (CTR). Here we report solution-state nuclear magnetic resonance (NMR) spectroscopy investigations of the conformation and dynamics of the disordered and flexible CTR of human HSP27, a systemically expressed sHSP. We observed multip...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1007/s12192-017-0791-z

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
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Institution:
University of Oxford
Oxford college:
University College
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
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Funding agency for:
Alderson, T
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Funding agency for:
Benesch, J
Grant:
EP/J01835X/1
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Funding agency for:
Baldwin, A
Grant:
David Phillips Fellowship BB/J014346/1
Publisher:
Springer Verlag Publisher's website
Journal:
Cell Stress and Chaperones Journal website
Volume:
22
Issue:
4
Pages:
639–651
Publication date:
2017-05-25
Acceptance date:
2017-03-24
DOI:
EISSN:
1466-1268
ISSN:
1355-8145
Source identifiers:
697936
Language:
English
Keywords:
Pubs id:
pubs:697936
UUID:
uuid:37ad6bf2-2907-44c4-bb59-406db1f5b7fd
Local pid:
pubs:697936
Deposit date:
2017-06-08

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