Mutation of the proteolytic cleavage site enhances stability and yield of recombinant hepatitis C virus core protein in bacterial cells.

Abstract excerpt

The Hepatitis C virus (HCV) core protein is crucial for viral assembly and pathogenesis; however, structural studies have been hampered by its instability and historical reliance on denaturing purification methods. Although a recent non-denaturing purification method for an E. coli-expressed HCV core 1-164 protein enabled initial characterization, the purified protein exhibited poor long-term stability owing to...

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