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

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Date

2011

Authors

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

Journal Title

Journal ISSN

Volume Title

Publisher

John Wiley & Sons Inc

Abstract

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

Description

Keywords

Keywords: Amyloid disease; Amyloid fibril; Chaperone activity; Covalent binding; Covalent immobilization; Covalently bound; Dialysis-related amyloidosis; Dry mass; In-vitro; Lysine residues; Misfolded proteins; molecular chaperone; Molecular chaperones; Partial unf covalent immobilization; molecular chaperone; small heat-shock protein

Citation

URI

http://hdl.handle.net/1885/63319

Collections

ANU Research Publications

Source

Biopolymers

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1002/bip.21584

Restricted until

2037-12-31

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Description
01_Garvey_Enhanced_molecular_chaperone_2011.pdf (1.24 MB)

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