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Reports of Biochemistry & Molecular Biology
Recombinant proteins overexpressed in E. coli are usually deposited in inclusion bodies. Cysteines in the protein contribute to this process. Inter-and intra-molecular disulfide bonds in chitinase, a cysteine-rich protein, cause aggregation when the recombinant protein is overexpressed in E. coli. Hence, aggregated proteins should be solubilized and allowed to refold to obtain native-or correctly-folded recombinant proteins. Methods: Dilution method that allows refolding of recombinantfatcat:scdlfvdw4neixba3tmpxmuqr4a