Approaches to the isolation and characterization of molecular chaperones
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 Creutz...
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| Veröffentlicht in: | Protein expression and purification 2006-03, Vol.46 (1), p.1-15 |
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| container_title | Protein expression and purification |
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| creator | Nicoll, William S. Boshoff, Aileen Ludewig, Michael H. Hennessy, Fritha Jung, Martin Blatch, Gregory L. |
| description | 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. |
| doi_str_mv | 10.1016/j.pep.2005.08.005 |
| format | Article |
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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. 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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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16199180</pmid><doi>10.1016/j.pep.2005.08.005</doi><tpages>15</tpages></addata></record> |
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| subjects | Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Affinity chromatography Alzheimer Disease - metabolism ATPase activity Codon optimization/harmonization Complementation assays Creutzfeldt-Jakob Syndrome - metabolism DnaJ DnaK Endoplasmic Reticulum - metabolism Enzymes - chemistry Enzymes - isolation & purification Heat shock proteins Hsp40 Hsp70 HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - metabolism Humans Molecular Chaperones - chemistry Molecular Chaperones - isolation & purification Molecular Chaperones - metabolism Molecular chaperones of the endoplasmic reticulum Protein Conformation Protein Folding Recombinant Proteins - metabolism |
| title | Approaches to the isolation and characterization of molecular chaperones |
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