Microsecond Resolution of Single-Molecule Rotation Catalyzed by Molecular Motors

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

doi:10.1007/978-1-61779-261-8_18

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 proceeding › Chapter

13 Scopus citations

Abstract

Single-molecule measurements of rotation catalyzed by the F₁-ATPase or the F_oF₁ ATP synthase have provided new insights into the molecular mechanisms of the F₁ and F_o molecular motors. We recently developed a method to record ATPase-driven rotation of F₁ or F_oF₁ 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 language	English (US)
Title of host publication	Single Molecule Enzymology
Subtitle of host publication	Methods and Protocols
Publisher	Humana Press Inc.
Pages	273-289
Number of pages	17
ISBN (Print)	9781617792601
DOIs	https://doi.org/10.1007/978-1-61779-261-8_18
State	Published - 2011

Publication series

Name	Methods in Molecular Biology
Volume	778
ISSN (Print)	1064-3745
ISSN (Electronic)	1940-6029

Keywords

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

ASJC Scopus subject areas

Genetics
Molecular Biology

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10.1007/978-1-61779-261-8_18

Cite this

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title = "Microsecond Resolution of Single-Molecule Rotation Catalyzed by Molecular Motors",

abstract = "Single-molecule measurements of rotation catalyzed by the F1-ATPase or the FoF1 ATP synthase have provided new insights into the molecular mechanisms of the F1 and Fo molecular motors. We recently developed a method to record ATPase-driven rotation of F1 or FoF1 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.",

keywords = "Dark field microscopy, F-ATPase, FF ATP synthase, Gold nanorods, Molecular motors, Nanodiscs, Plasmon resonance, Single molecule",

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AU - Martin, James

AU - Spetzler, David

AU - Ishmukhametov, Robert

AU - Frasch, Wayne

PY - 2011

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AB - Single-molecule measurements of rotation catalyzed by the F1-ATPase or the FoF1 ATP synthase have provided new insights into the molecular mechanisms of the F1 and Fo molecular motors. We recently developed a method to record ATPase-driven rotation of F1 or FoF1 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.

KW - Dark field microscopy

KW - F-ATPase

KW - FF ATP synthase

KW - Gold nanorods

KW - Molecular motors

KW - Nanodiscs

KW - Plasmon resonance

KW - Single molecule

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Microsecond Resolution of Single-Molecule Rotation Catalyzed by Molecular Motors

Abstract

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