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Wednesday, April 26 • 8:30am - 10:00am
Reconstitution of E. coli F1FO into artificial membranes to examine the effects of lipid composition

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ATP synthase catalyzes the synthesis of adenosine triphosphate by use of two rotary, designated F1 and FO, within the F1FO complex. ATP is the primary carrier of chemical energy in all life forms. The membrane-embedded FO motor uses a H+ gradient created by the electron transport chain to drive rotation of the c ring, which drives the conformational changes within the subunits α and β subunits of the F1 motor that catalyze ADP and phosphate into ATP. The mechanism of how the protons flow through ATP synthase to generate the torque on the c-ring remains unclear. Prior research has shown that the lipid composition of the membrane can influence the functions of the proteins embedded within it. To examine the effects of lipid composition on ATP synthase, the F1F0 complex was purified out of E. coli cells and tested for ATPase activity. F1FO will be reconstituted back into liposomes with varying lipid composition, especially focusing on the concentration of phosphatidylethanolamine, which is usually found in the membranes of E. coli. The ultimate objective of this project is to see if the presence or lack of specific lipids has any effect on ATP synthesis.


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

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