CHED 784 |
| Small molecules incorporating lanthanide ions have been known since the early 1990's to hydrolytically cleave DNA. However it remains difficult to design nucleases with the potential to cleave specific sequences of choice. Nucleases with this ability would prove to be invaluable in the biochemical and pharmaceutical professions. Several previous research groups have been successful in metalloprotein design by incorporating protein scaffolds. The protein of interest was designed by Welch et al. The protein binds lanthanide ions, has a metal-dependent structure, and catalyzes hydrolysis of phosphate esters and supercoiled DNA. Welch et al created this nuclease synthetically and examined its ability to bind metal and cleave DNA. The purpose of this experiment is to investigate the effects of synthetic creation vs. biological creation. Biological construction is potentially more economical for the production of the protein and variants. In order to do this the P4a nuclease will be created using biological construction methods and tested in a similar manner. If this nuclease functions independent of the way in which it was created similar binding affinity and cleavage rates are expected. |
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Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |