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- W2042853008 abstract "One major challenge in the expression and purification of recombinant proteins is preventing proteins from forming inclusion bodies. Recovery of proteins from inclusion bodies can be laborious, and often a futile exercise. The partition between productive folding and non-specific aggregation/inclusion body formation is believed to be a competition between non-specific and specific structural interactions. Aggregation/inclusion body formation can be thwarted by promoting conditions that facilitate specific interactions during folding of the polypeptide chain.D2 module of the extracellular immunoglobulin-like domain of the fibroblast growth factor (FGF) is overexpressed in Escherichia coli as inclusion bodies. Urea denaturation of inclusion bodies, and subsequent refolding, results in meager yields of the recombinant protein. In addition, the “nativity” of the refolded recombinant D2 module is always questionable. In this context, we have designed a novel Duet vector that co-expresses the D2 module and the ligand (FGF) simultaneously. It is predicted that the receptor module and FGF will form a soluble binary complex which can be dissociated under high salt conditions to simultaneously yield pure recombinant D2 module and FGF. Using the purified recombinant proteins, the structure of the FGF-receptor complex will be characterized using a variety of biophysical experiments, including multidimensional NMR spectroscopy." @default.
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- W2042853008 date "2011-02-01" @default.
- W2042853008 modified "2023-09-27" @default.
- W2042853008 title "Design of a Duet Expression Vector to Characterize Ligand-receptor Interactions" @default.
- W2042853008 doi "https://doi.org/10.1016/j.bpj.2010.12.497" @default.
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