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Enhanced molecular chaperone activity of a small heat-shock αΒprotein following covalent immobilization onto a solid-phase support

Garvey, Megan; Griesser, Stefani S.; Griesser, Hans; Thierry, Benjamin; Nussio, Matthew R.; Shapter, Joseph G; Ecroyd, Heath; Giorgetti, Sofia; Bellotti, Vittorio; Gerrard, Juliet A.; Carver, John

Description

The well-characterized small heat-shock protein, αB-crystallin, acts as a molecular chaperone by interacting with unfolding proteins to prevent their aggregation and precipitation. Structural perturbation (e.g., partial unfolding) enhances the in vitro c

CollectionsANU Research Publications
Date published: 2011
Type: Journal article
URI: http://hdl.handle.net/1885/63319
Source: Biopolymers
DOI: 10.1002/bip.21584

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