Microsecond resolution of single-molecule rotation catalyzed by molecular motors

Tassilo Hornung, James Martin, David Spetzler, Robert Ishmukhametov, Wayne Frasch

Research output: Chapter in Book/Report/Conference proceedingChapter

10 Scopus citations

Abstract

Single-molecule measurements of rotation catalyzed by the F 1-ATPase or the F oF 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 oF 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.

Original languageEnglish (US)
Title of host publicationSingle Molecule Enzymology
Subtitle of host publicationMethods and Protocols
EditorsGregory I. Mashanov, Christopher Batters
Pages273-289
Number of pages17
DOIs
StatePublished - Oct 24 2011

Publication series

NameMethods in Molecular Biology
Volume778
ISSN (Print)1064-3745

Keywords

  • Dark field microscopy
  • F -ATPase
  • F F ATP synthase
  • Gold nanorods
  • Molecular motors
  • Nanodiscs
  • Plasmon resonance
  • Single molecule

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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  • Cite this

    Hornung, T., Martin, J., Spetzler, D., Ishmukhametov, R., & Frasch, W. (2011). Microsecond resolution of single-molecule rotation catalyzed by molecular motors. In G. I. Mashanov, & C. Batters (Eds.), Single Molecule Enzymology: Methods and Protocols (pp. 273-289). (Methods in Molecular Biology; Vol. 778). https://doi.org/10.1007/978-1-61779-261-8_18