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Approaches to the isolation and characterization of molecular chaperones

Nicoll, William S, Boshoff, Aileen, Ludewig, Michael H, Hennessy, Fritha, Jung, Martin and Blatch, Gregory L (2006) Approaches to the isolation and characterization of molecular chaperones. Protein Expression and Purification, 46 (1). pp. 1-15. ISSN 1046-5928

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Abstract

Molecular chaperones are integral components of the cellular machinery involved in ensuring correct protein folding and the continued maintenance of protein structure. An understanding of these ubiquitous molecules is key to finding cures to protein misfolding diseases such as Alzheimer’s and Creutzfeldt–Jacob diseases. In addition, further understanding of chaperones will enhance our comprehension of the way the body copes with the environmental stresses that humans encounter daily. Our laboratory and our collaborators specialize in the production and characterization of chaperones from a wide variety of sources in order to gain a fuller understanding of how chaperones function in the cell. In this review, we primarily use the Hsp70/Hsp40 chaperone pair as an example to discuss recent advances in technology and reductions in cost that lend themselves to chaperone purification from both native and recombinant sources. Common assays to assess purified chaperone activity are also discussed.

Item Type: Article
Additional Information:

Online ISSN: 1096-0279

Uncontrolled Keywords: ResPubID22211. heat shock proteins, heat sensitive proteins, Hsp70, Hsp40, DnaK, DnaJ, genetics, molecular chaperones of the endoplasmic reticulum, affinity chromatography, codon optimisation, condon harmonisation, ATPase activity, complementation assays
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 1101 Medical Biochemistry and Metabolomics
Depositing User: VUIR
Date Deposited: 02 Feb 2012 00:16
Last Modified: 23 Mar 2015 05:17
URI: http://vuir.vu.edu.au/id/eprint/8156
DOI: https://doi.org/10.1016/j.pep.2005.08.005
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Citations in Scopus: 18 - View on Scopus

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