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

Internet

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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