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The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated.

Abstract:

The function of ScHSP26 is thermally controlled: the heat shock that causes the destabilization of target proteins leads to its activation as a molecular chaperone. We investigate the structural and dynamical properties of ScHSP26 oligomers through a combination of multiangle light scattering, fluorescence spectroscopy, NMR spectroscopy, and mass spectrometry. We show that ScHSP26 exists as a heterogeneous oligomeric ensemble at room temperature. At heat-shock temperatures, two shifts in equi...

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Publication status:
Published
Peer review status:
Peer reviewed

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author
Publisher:
Cell Press
Journal:
Chemistry and biology More from this journal
Volume:
17
Issue:
9
Pages:
1008-1017
Publication date:
2010-09-01
DOI:
EISSN:
1879-1301
ISSN:
1074-5521

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