Refolding of Inclusion Body Proteins

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Abstract

Genome sequencing projects have led to the identification of an enormous number of open reading frames that code for unknown proteins. Elucidation of the structure and function of these proteins makes it necessary to produce proteins fast, in high yields and at low cost. The recombinant expression of proteins in bacterial hosts often results in the formation of inclusion bodies. Here, the protein accumulates in large quantities separated from the cellular protein. However, the protein is insoluble and inactive. Thus, it is necessary to establish efficient refolding protocols. Progress has been made recently in this field concerning refolding strategies, the use of low-molecular-weight additives as folding enhancers, and the determination of optimum refolding parameters. Here we present an overview of the refolding technology and give a standard protocol for inclusion body refolding.