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[Refolding of recombinant proteins in vitro].

Jianyin Long, H X Wang

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Abstract

Refolding of recombinant proteins is an important event in the downstream process of genetic engineering. On the basis of the mechanism of protein folding in vitro, general strategy of recombinant protein refolding is postulated, and major developments in recent years on this field are reviewed, including: molecular chaperone mediated refolding, detergent-assisted refolding, protein refolding in reverse micelle, addition of folding enhancer and methods for the formation of disulfide bond during protein refolding.

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Refolding of recombinant proteins is an important event in the downstream process of genetic engineering. On the basis of the mechanism of protein folding in vitro, general strategy of recombinant protein refolding is postulated, and major developments in recent years on this field are reviewed, including: molecular chaperone mediated refolding, detergent-assisted refolding, protein refolding in reverse micelle, addition of folding enhancer and methods for the formation of disulfide bond during protein refolding.

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Available abstract

Refolding of recombinant proteins is an important event in the downstream process of genetic engineering. On the basis of the mechanism of protein folding in vitro, general strategy of recombinant protein refolding is postulated, and major developments in recent years on this field are reviewed, including: molecular chaperone mediated refolding, detergent-assisted refolding, protein refolding in reverse micelle, addition of folding enhancer and methods for the formation of disulfide bond during protein refolding.

Key concepts: Recombinant DNA, Protein folding, Chemistry, Chaperone (clinical), In vitro, Micelle, Protein aggregation, Folding (DSP implementation)

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