Approaches to the isolation and characterization of molecular chaperones

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Nicoll, William S, Boshoff, Aileen, Ludewig, Michael H, Hennessy, Fritha, Jung, Martin and Blatch, Gregory ORCID: 0000-0003-0778-8577 (2006) Approaches to the isolation and characterization of molecular chaperones. Protein Expression and Purification, 46 (1). pp. 1-15. ISSN 1046-5928


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.

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Online ISSN: 1096-0279

Item type Article
DOI 10.1016/j.pep.2005.08.005
Official URL
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 1101 Medical Biochemistry and Metabolomics
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
Citations in Scopus 18 - View on Scopus
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