Evaluating the effect of phosphorylation on the structure and dynamics of Hsp27 dimers by means of ion mobility mass spectrometry

Evaluating the effect of phosphorylation on the structure and dynamics of Hsp27 dimers by means of ion mobility mass spectrometry

The quaternary structure and dynamics of the human small heat-shock protein Hsp27 are linked to its molecular chaperone function and influenced by post-translational modifications, including phosphorylation. Phosphorylation of Hsp27 promotes oligomer dissociation and can enhance chaperone activity....

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Autors principals:	Jovcevski, B, Kelly, M, Aquilina, J, Benesch, J, Ecroyd, H
Format:	Journal article
Idioma:	English
Publicat:	American Chemical Society 2017

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