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My trip to Boston was not the smoothest journey I could have hoped for. I left from Tucson at 7 AM (10 AM Eastern), and after numerous airport delays, a missed flight, baggage troubles, and a lost cab driver, I arrived at my room 15 hours later at 1 AM. However, since my initial long trip, I have been having a great time in Cambridge and Boston. Before this summer, the furthest east I had been was Dallas, and I have really been enjoying my time on the east coast. The weather here has been really nice, usually in the upper 70's or lower 80's, but it can be quite humid. The people I have met in my program, both fellow students and MIT faculty, have been really great, interesting people, and I feel like I am gaining a great deal of knowledge and friends from this summer program. |
| I am working at MIT as part of the MSRP biology program that is funded primarily through the Howard Hughes Medical Institute. I am doing research in Dr. Robert Sauer's laboratory in the Koch Biology building, and I am working on a project together with a post doctorate student, Jungsan "J" Sohn, who received his Ph.D. from Duke University . We are studying a protease from Escherichia coli, DegS, which is the initial protein involved in the release of the transcription factor, sE, which regulates the periplasmic stress response in E. coli . sE regulates the expression of chaperones, proteases, and enzymes involved in lipid syntheses which are necessary during stress that is most often caused by elevated temperatures. DegS is a trimer with each monomer consisting of a PDZ domain and a serine protease domain similar to trypsin. The PDZ domain regulates the protease domain because the PDZ domain must first bind to the C-terminal peptide of an outer membrane porin (OMP) before the protease domain can become active. |
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I am using site-directed mutagenesis to study the important amino acid residues that are involved in peptide binding to the PDZ domain and subsequent activation of the protease domain. Fluorescence anisotropy is used to quantify the binding characteristics of the mutants that we generate, and these are compared with wild type binding. Also, SDS-PAGE allows us to qualitatively observe the activation of the protein. Furthermore, I am also attempting to crystallize the wild type DegS protein so that we can observe changes in the protein's structure when different peptides are bound. With this information, we can try to understand how the protein gets activated and what residues or shifts in the protein are important for the protease to go from inactive to active. |
| Besides doing research, I have been having fun with the other members of the program visiting sites in Cambridge and Boston . A group of us rented cars and went to Six Flags New England one weekend which was really fun except for the rain that we had towards the end of the day. The program also coordinated a trip to Martha's Vineyard which was really nice, and it was the first time that I ever swam in the Atlantic Ocean . Also, I am enjoying the active sports communities at MIT. There are pick-up soccer games every day that I join from time to time, and I go running often which seems to be a popular activity. Any time of day there seems to be people running. I have a few more weeks left in the program, and I hope to make the most of them. I have been having a great time, but I also look forward to returning to Tucson and the U of A. |
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