2001Letters in BiotechnologyRequires access

Advance in vitro folding of inclusion body proteins

Yun Ning

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Abstract

Expression of recombinant proteins as inclusion bodies in bacteria is one of the most efficient ways to produce cloned proteins, however, the product of interest is frequently deposited in insoluble inactive aggregates or inclusion bodies. Aggregation is the leading cause of decreased refolding yields. Understanding of the mechanism of aggregation is very important to establish efficient refolding process. Renaturation yield of recombinant protein have been improved by using some additives, such as molecular chaperone, small molecules that interfere with intermolecular interactions responsible for aggregation.

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What this paper is about

Expression of recombinant proteins as inclusion bodies in bacteria is one of the most efficient ways to produce cloned proteins, however, the product of interest is frequently deposited in insoluble inactive aggregates or inclusion bodies. Aggregation is the leading cause of decreased refolding yields. Understanding of the mechanism of aggregation is very important to establish efficient refolding process. Renaturation yield of recombinant protein have been improved by using some additives, such as molecular chaperone, small molecules that interfere with intermolecular interactions responsible for aggregation.

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Available abstract

Expression of recombinant proteins as inclusion bodies in bacteria is one of the most efficient ways to produce cloned proteins, however, the product of interest is frequently deposited in insoluble inactive aggregates or inclusion bodies. Aggregation is the leading cause of decreased refolding yields. Understanding of the mechanism of aggregation is very important to establish efficient refolding process. Renaturation yield of recombinant protein have been improved by using some additives, such as molecular chaperone, small molecules that interfere with intermolecular interactions responsible for aggregation.

Key concepts: Inclusion bodies, Recombinant DNA, Chaperone (clinical), Protein aggregation, Protein folding, Chemistry, In vitro, Chemical chaperone

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