Local unfolding of the HSP27 monomer regulates chaperone activity

The small heat-shock protein HSP27 occurs predominantly in oligomeric forms, which makes its structural characterisation challenging. Here the authors employ CPMG and high-pressure NMR with native mass spectrometry and biophysical assays to show that the active monomeric form of HSP27 is substantial...

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Autores principales: T. Reid Alderson, Julien Roche, Heidi Y. Gastall, David M. Dias, Iva Pritišanac, Jinfa Ying, Ad Bax, Justin L. P. Benesch, Andrew J. Baldwin
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/550a85efe9614ed0b28d5ac8d6498385
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