论文部分内容阅读
Protein infolding is an indispensable process in the production of recombinant proteins expressed as inclusion bodies in host bacteria.To enable the rational design of an optimal solution environment for infolding by using chemical additives, we employed two approaches: the effect of a series of water-soluble ionic liquids on refolding process was elaborately investigated to understand the manner in which their chemical structures confer suitable properties for protein refolding.Next, we showed that the further addition of organic cosolvents can modulate the interaction between conventional refolding additives and protein to drastically enhance the refolding yields.These outcomes of our approaches are expected to have potential application to the refolding process of a wide variety of proteins.