Open AccessReactivation of Aggregated Proteins by the ClpB/DnaK Bi‐Chaperone System
Author(s) -
Zolkiewski Michal,
Chesnokova Liudmila S.,
Witt Stephan N.
Publication year - 2016
Publication title -
current protocols in protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.409
H-Index - 32
eISSN - 1934-3663
pISSN - 1934-3655
DOI - 10.1002/0471140864.ps2810s83
Subject(s) - clpb , chaperone (clinical) , escherichia coli , protein aggregation , biochemistry , protein folding , escherichia coli proteins , biology , enzyme , chemistry , microbiology and biotechnology , gene , medicine , pathology
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.