Chaperon Proteins and Disulfide Bond Isomerase

Chaperon Proteins and Disulfide Bond Isomerase

DnaK (HSP70)

DnaK is the prokaryotic analogue of eukaryotic Hsp70, a member of the heat shock proteins. It assists the protein assembly, folding, and translocation. 

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GroEL
The bacterial chaperonin GroEL is a double toroidal assembly, which together with the action of the ring-shaped oligomeric cochaperonin, GroES, facilitates protein folding in an ATP dependent manner.
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GroES
GroES protein is a chaperonin family protein that works in conjunction with GroEL to facilitate proper protein folding. GroES consists of 7 subunits with a molecular weight of 10.4kDA. The recombinant full length protein was overexpression in E.coli and purified by chromatography.
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PDI1 (yeast)
Recombinant yeast PDI is produced in E.coli is as single, non-glycosylated, polypeptide chain containing 503 amino acids and having a molecular mass of 62.4 kDa. The PDI is fused to a 12 amino acid His-tag (515 a.a. total) at N-terminal and purified by proprietary chromatographic techniques.
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