Heterologous proteins produced by recombinant DNA technology are frequently isolated in unfolded and inactive forms. These proteins must be refolded before a useful product is obtained. In this proposal, a novel quasi-electric light scattering (QELS) technique is proposed for use in studying protein refolding and aggregation. Processing conditions that facilitate protein refolding and environmental effects on the functional properties of the folded proteins will be evaluated using beta-galactosidase as a model protein.
