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
DOIAbstract
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
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