ORGN 391 |
| The poly-His tag is often expressed on fusion proteins to aid in protein isolation and purification. However, the poly-His tag can also lead to misfolding and low protein solubility. We have found that cleavage of poly-His tags is impeded by protein secondary structures. Our bZIP proteins form a dimeric coiled-coil structure. Taking advantage of this fact, we have designed a short peptide as a dimerization agent to target structure subdomains. This alternative strategy has allowed enterokinase to perform efficient proteolysis of the poly-His tags. |
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New Reactions and Methodology, Bioorganic Chemistry, Molecular Recognition and Self Assembly
8:00 PM-10:00 PM, Tuesday, 28 March 2006 Georgia World Congress Center -- Ex. Hall B4, Poster
Sci-Mix
Division of Organic Chemistry |