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Mechanism of the F1 ATPase Molecular Motor as Revealed by Single Molecule Studies


Abstract The F1Fo ATP synthase is required for energy conversion in almost all living organisms. The F1 complex is a molecular motor that uses ATP hydrolysis to drive rotation of the γ–subunit. It has not been previously possible to resolve the speed and position of the γ–subunit of the F1–ATPase as it rotates during a power stroke. The single molecule experiments presented here measured light scattered from 45X91 nm gold nanorods attached to the γ–subunit that provide an unprecedented 5 μs resolution of rotational position as a function of time. The product of velocity and drag, which were both measured directly, resulted in an average torque of 63±8 pN nm for t... (more)
Created Date 2012
Contributor Martin Ii, James Leo (Author) / Frasch, Wayne D (Advisor) / Chandler, Douglas (Committee member) / Gaxiola, Roberto (Committee member) / Yan, Hao (Committee member) / Arizona State University (Publisher)
Subject Biophysics / Biochemistry / F1-ATPase / gold nanorod / molecular motor / single molecule / torque
Type Doctoral Dissertation
Extent 180 pages
Language English
Copyright
Reuse Permissions All Rights Reserved
Note Ph.D. Molecular and Cellular Biology 2012
Collaborating Institutions Graduate College / ASU Library
Additional Formats MODS / OAI Dublin Core / RIS


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Description Dissertation/Thesis