CHED 951 |
| Methyl-accepting chemotaxis proteins (MACPs) provide a good model for the human drug receptors. MACPs are part of a sensitive sensing and signaling system that is capable of detecting slight differences in ligand concentration. Current research shows that these bacterial receptors organize into trimer of dimers at the tip of their signaling domain. To confirm this organization, a photocrosslinking unnatural amino acid, p-benzoylphenylalanine, was added to the tip of the signaling region of the serine chemoreceptor. The mutant receptor was crosslinked to any touching receptors and visualized using Western Blotting. It has also been found that receptors organize into mixed receptor squads, which can be verified by crosslinking in a cell line containing the other chemoreceptors. Swarm assays were utilized to determine whether the addition of the unnatural amino acid influenced receptor function. In order to elucidate the conformational change that propagates the signal across the bacterial cell membrane, the crosslinking amino acid was added to the transmembrane region in a similar fashion and crosslinked. From crosslinking analysis it is possible to determine the conformational change that carries the signal. |
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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 |