title: Microsecond resolution of single-molecule rotation catalyzed by molecular motors.
abstract: Single-molecule measurements of rotation catalyzed by the F(1)-ATPase or the F(o)F(1) ATP synthase have provided new insights into the molecular mechanisms of the F(1) and F(o) molecular motors. We recently developed a method to record ATPase-driven rotation of F(1) or F(o)F(1) in a manner that solves several technical limitations of earlier approaches that were significantly hampered by time and angular resolution, and restricted the duration of data collection. With our approach it is possible to collect data for hours and obtain statistically significant quantities of data on each molecule examined with a time resolution of up to 5 μs at unprecedented signal-to-noise.
authors.affiliation: Faculty of Biomedicine and Biotechnology, School of Life Sciences, Arizona State University, Tempe, AZ, USA.
authors.forename: Tassilo
authors.initials: T
authors.lastname: Hornung
authors.forename: James
authors.initials: J
authors.lastname: Martin
authors.forename: David
authors.initials: D
authors.lastname: Spetzler
authors.forename: Robert
authors.initials: R
authors.lastname: Ishmukhametov
authors.forename: Wayne D
authors.initials: WD
authors.lastname: Frasch
mesh_terms: D006046:Gold / Q000737:chemistry; D008853:Microscopy; D025261:Mitochondrial Proton-Translocating ATPases / Q000378:metabolism; D020409:Molecular Motor Proteins / Q000378:metabolism*; D036103:Nanotechnology / Q000379:methods*; D043942:Nanotubes / Q000737:chemistry; D006180:Proton-Translocating ATPases / Q000378:metabolism
chemical_list: D020409:Molecular Motor Proteins; D006046:Gold; C474451:F1F0-ATP synthase; D025261:Mitochondrial Proton-Translocating ATPases; D006180:Proton-Translocating ATPases