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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Authors
Funding
+ Biotechnology and Biological Sciences Research Council
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Funding agency for:
Baldwin, A
Grant:
David Phillips Fellowship BB/J014346/1
+ Engineering and Physical Sciences Research Council
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Funding agency for:
Benesch, J
Grant:
EP/J01835X/1
+ National Institute of Diabetes and Digestive and Kidney Diseases
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Funding agency for:
Alderson, T
Bibliographic Details
- 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
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:697936
- UUID:
-
uuid:37ad6bf2-2907-44c4-bb59-406db1f5b7fd
- Local pid:
- pubs:697936
- Source identifiers:
-
697936
- Deposit date:
- 2017-06-08
Terms of use
- Copyright holder:
- Alderson et al
- Copyright date:
- 2017
- Notes:
- © The Author(s) 2017. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License.
- Licence:
- CC Attribution (CC BY)
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