CHED 956 |
| The halogen bonding interactions have yet to be explored in protein stabilization. Here we present the first study comparing the effects of halogen bonds versus hydrogen bonds in protein folding, stability. Site directed mutagenesis and nonsense suppression with specialized tRNA synthetases has allowed incorporation of these UAAs and tyrosine in T4 Lysosyme. The modified T4 lysozyme has been generated by replacing Phe104 with tyrosine, bromophenylalanine, iodophenylalanine, and trifluoromethylphenylalanine. The unnatural amino acid incorporation has been verified via trypsin digest and mass spectrometry. The effects of these modifications on structural and thermal stability will be examined by measuring the melting point of the mutant constructs and crystal structure analysis. |
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Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, March 26, 2007 Hyatt Regency Chicago -- Riverside Center, Poster
Division of Chemical Education |