CTS-9502235 Roger Harrison U of Oklahoma Research will be performed to improve the purification of recombinant proteins by avoiding the initial expression of these proteins as insoluble inclusion bodies. A primary goal is to test new fusion proteins that are predicted to enhance the solubility of normally insoluble recombinant proteins. Four proteins with very high solubility in Escherichia coli will be combined with two different target proteins known to have low solubility. The fusion proteins with highest expression levels will be purified. The target protein will be purified after its cleavage from the fusion protein and characterized further. The experiments will test the validity of a model proposed to predict the solubility of fusion proteins. The results may lead to fundamental advances in fusion protein technology which could have significant impact in biotechnology.
