The Quaternary Organization and Dynamics of the Molecular Chaperone HSP26 Are Thermally Regulated

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, fluor...

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Hoofdauteurs: Benesch, Justin L.P., Aquilina, J. Andrew, Baldwin, Andrew J., Rekas, Agata, Stengel, Florian, Lindner, Robyn A., Basha, Eman, Devlin, Glyn L., Horwitz, Joseph, Vierling, Elizabeth, Carver, John A., Robinson, Carol V.
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 2010
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3388541/
https://ncbi.nlm.nih.gov/pubmed/20851350
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.chembiol.2010.06.016
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