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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Quaternary dynamics and plasticity underlie small heat shock protein chaperone function.

Florian Stengel1, Andrew J Baldwin, Alexander J Painter

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|February 6, 2010
PubMed
Summary

Small Heat Shock Proteins (sHSPs) prevent cellular damage by binding to stressed proteins. Their complex structures and dynamics reveal a novel mechanism for maintaining protein homeostasis.

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