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C-terminal interactions mediate the quaternary dynamics of αB-crystallin

αB-crystallin is a highly dynamic, polydisperse small heat-shock protein that can form oligomers ranging in mass from 200 to 800 kDa. Here we use a multifaceted mass spectrometry approach to assess the role of the C-terminal tail in the self-assembly of αB-crystallin. Titration experiments allow us...

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Detalles Bibliográficos
Autores principales:	Hilton, Gillian R., Hochberg, Georg K. A., Laganowsky, Arthur, McGinnigle, Scott I., Baldwin, Andrew J., Benesch, Justin L. P.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	The Royal Society 2013
Materias:	Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3638394/ https://www.ncbi.nlm.nih.gov/pubmed/23530258 http://dx.doi.org/10.1098/rstb.2011.0405

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