Unit

UNIT 28.10 Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System

  1. Michal Zolkiewski1,
  2. Liudmila S. Chesnokova2,
  3. Stephan N. Witt3

Published Online: 2 FEB 2016

DOI: 10.1002/0471140864.ps2810s83

Lab Protocol Title

Current Protocols in Protein Science

Current Protocols in Protein Science

Additional Information

How to Cite

Zolkiewski, M., Chesnokova, L.S., and Witt, S.N. 2016. Reactivation of aggregated proteins by the ClpB/DnaK Bi-chaperone system. Curr. Protoc. Protein Sci. 83:28.10.1-28.10.18. doi: 10.1002/0471140864.ps2810s83

Author Information

  1. 1

    Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas

  2. 2

    Department of Microbiology and Immunology, Louisiana State University Health Sciences Center, Shreveport, Louisiana

  3. 3

    Department of Biochemistry and Molecular Biology and Department of Pharmacology, Toxicology and Neuroscience, Louisiana State University Health Sciences Center, Shreveport, Louisiana

Publication History

  1. Published Online: 2 FEB 2016
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Abstract

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. © 2016 by John Wiley & Sons, Inc.

Keywords:

  • protein misfolding;
  • protein aggregation;
  • molecular chaperone;
  • ClpB;
  • DnaK
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