CHED 941 |
| Protein-protein interactions are vital to biological pathways, mediating many fundamental biological processes ranging from formation of hormone-receptor complexes to programmed cell death. Many studies have been recently directed towards protein interface because the interface is involved with complex assemblies, allosteric interactions, protein stability and important signaling events. Recently, a photoreactive amino acid, p-benzoyl-L-phenyalanine (Bpa), has been employed to identify protein-protein interactions and to map specific protein-protein contact points. The orthogonal pair of tRNABpaCUA and MjBpa-RS synthetase was reported to incorporate Bpa at the TAG site with high fidelity. The difficulty in designing successful photocrosslinking experiments is compounded by the lack of literature relating the protein environments to the observed photocrosslinking results. This study aims to cover this gap of knowledge by determining to what extent the interface environments affects the photochemistry of Bpa in vitro and in vivo as well as how the covalent crosslinks alter the interface and the protein. Here we present a comparison of photocrosslinking at different interface sizes and hydrophilicities in vitro and in vivo in order to determine the optimal conditions for the photoreaction and the effects of Bpa on the interface structure and protein stability. |
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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 |