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Wednesday, April 26 • 8:30am - 10:00am
Chemical and genetic modification of key sites in E. coli F1FO ATP Synthase.

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ATP Synthase is a complex integral membrane protein consisting of two rotary motors: the FO portion, which is embedded in the cell membrane, and the F1 portion, which is located on the inside of the cell. ATP synthase is the primary generator of adenosine triphosphate (ATP), which is an energy rich molecule required for a variety of critical cellular functions. As important as ATP synthase is, the mechanics of exactly how it works are still not completely known. The FO rotor transduces an electrochemical gradient of protons into mechanical rotation of an oligomeric ring of c subunits. Several amino acids, e.g. phenylalanine 54 (F54), have been identified within subunit c that, when mutated to cysteine, have shown to allow synthesis of ATP while inhibiting ATP-driven proton pumping. I plan to chemically and genetically alter the structure of these amino acids to try to understand the specific characteristics that affect subunit c’s function. The addition of a propyl group to the cysteine side chain at the F54 position has shown to restore some function in the ATP-driven proton pumping direction. These results suggest that hydrophobic bulk may have a functional role at that position.

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Wednesday April 26, 2017 8:30am - 10:00am
Concourse - Wilma Sherrill Center

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