Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System
| Autor: | Michal Zolkiewski, Liudmila S. Chesnokova, Stephan N. Witt |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Endopeptidase Clp Protein aggregation Glucosephosphate Dehydrogenase medicine.disease_cause Biochemistry Article 03 medical and health sciences Protein Aggregates Structural Biology Heat shock protein medicine Escherichia coli Humans HSP70 Heat-Shock Proteins Heat-Shock Proteins biology Escherichia coli Proteins Protein Biochemistry Enzyme Activation 030104 developmental biology Solubility Chaperone (protein) biology.protein Protein folding CLPB |
| Zdroj: | Current Protocols in Protein Science |
| ISSN: | 1934-3663 |
| Popis: | Protein aggregation is a common problem in protein biochemistry and is linked to many cellular pathologies and human diseases. The molecular chaperone ClpB can resolubilize and reactivate aggregated proteins. This unit describes the procedure for following reactivation of an aggregated enzyme glucose-6-phosphate dehydrogenase mediated by ClpB from Escherichia coli in cooperation with another molecular chaperone, DnaK. The procedures for purification of these chaperones are also described. |
| Databáze: | OpenAIRE |
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