Thursday, January 20, 2005, 11:00 am — John Dunn Seminar Room, Bldg. 463
Many essential cellular functions are performed by nanoscale protein motors. The best-characterized of these is FoF1-ATP synthase, the smallest rotatory motor (known as the “engine for life”), which catalyzes ATP synthesis and hydrolysis with high efficiency under cellular conditions where ADP/Pi and ATP are present at similar concentrations. Although the binding change mechanism for F1-ATPase (i.e., the F1 domain of FoF1-ATP synthase) was proposed nearly two decades ago to explain how F1-ATPase functions, a detailed microscopic picture has not been clear. By computer simulation studies, we have developed a consistent model for ATP hydrolysis and synthesis in F1-ATPase. In this model, the essential steps of the chemical reactions and the mechanical motions are described and connected at molecular level. In addition, the physical aspects of F1-ATPase function such as energy usage and chemomechanical coupling are uncovered.
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