The rapid provision of purified native protein underpins both structural biology and the development of new biopharmaceuticals. The dominance of Escherichia coli as a cellular biofactory depends on technology for solubilizing And refolding proteins that are expressed as insoluble inclusion bodies. Such Technology must be scale invariant, easily automated, generic for a broad range Of similar proteins and economical. Refolding methods relying on denaturant Dilution and column-based approaches meet these criteria. Recent Developments, particularly in column-based methods, promise to extend the Range of proteins that can be refolded successfully.
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