Book section : Chapter
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.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
-
(Preview, Accepted manuscript, pdf, 963.6KB, Terms of use)
-
- Publisher copy:
- 10.1007/978-1-61779-261-8_18
Authors
- Publisher:
- Humana Press
- Host title:
- Single Molecule Enzymology: Methods and Protocols
- Pages:
- 273-289
- Series:
- Methods in Molecular Biology
- Series number:
- 778
- Place of publication:
- United States
- Publication date:
- 2011-01-01
- DOI:
- EISSN:
-
1940-6029
- ISSN:
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1064-3745
- Pmid:
-
21809213
- EISBN:
- 978-1-61779-261-8
- ISBN:
- 978-1-61779-260-1
- Language:
-
English
- Keywords:
- Subtype:
-
Chapter
- Pubs id:
-
167774
- Local pid:
-
pubs:167774
- Deposit date:
-
2023-07-28
Terms of use
- Copyright holder:
- Springer Science+Business Media, LLC
- Copyright date:
- 2011
- Rights statement:
- Copyright © 2011 Springer Science+Business Media, LLC
- Notes:
- This is the accepted manuscript version of the chapter. The final version is available online from Humana Press at https://dx.doi.org/10.1007/978-1-61779-261-8_18
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