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Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System.
Zolkiewski, Michal; Chesnokova, Liudmila S; Witt, Stephan N.
Afiliação
  • Zolkiewski M; Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas.
  • Chesnokova LS; Department of Microbiology and Immunology, Louisiana State University Health Sciences Center, Shreveport, Louisiana.
  • Witt SN; Department of Biochemistry and Molecular Biology and Department of Pharmacology, Toxicology and Neuroscience, Louisiana State University Health Sciences Center, Shreveport, Louisiana.
Curr Protoc Protein Sci ; 83: 28.10.1-28.10.18, 2016 Feb 02.
Article em En | MEDLINE | ID: mdl-26836408
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Choque Térmico HSP70 / Proteínas de Escherichia coli / Escherichia coli / Agregados Proteicos / Glucosefosfato Desidrogenase / Proteínas de Choque Térmico Idioma: En Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Choque Térmico HSP70 / Proteínas de Escherichia coli / Escherichia coli / Agregados Proteicos / Glucosefosfato Desidrogenase / Proteínas de Choque Térmico Idioma: En Ano de publicação: 2016 Tipo de documento: Article