Enhanced molecular chaperone activity of a small heat-shock αΒprotein following covalent immobilization onto a solid-phase support
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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
Collections | ANU Research Publications |
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Date published: | 2011 |
Type: | Journal article |
URI: | http://hdl.handle.net/1885/63319 |
Source: | Biopolymers |
DOI: | 10.1002/bip.21584 |
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