F1-ATPase:1分子でできた回転モーター
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Summary
This work has shown that F1 is a rotary motor by visualizing the rotation of a large marker attached to the putative rotator of this protein.
- Type
- article
- Published
- 1999-11-25
- Cited by
- 0
- References
- 12
- Access
- Open access
- OpenAlex
- https://openalex.org/W637154452
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:209590644
Keywords
ATP synthase, ATPase, Molecular motor, Rotation (mathematics), Rotary engine
References
- Single-molecule analysis of the actomyosin motor using nano-manipulation.
- The ATP synthase--a splendid molecular machine.
- Transcription Against an Applied Force
- Intramolecular rotation in ATP synthase: dynamic and crystallographic studies on thermophilic F1.
- Intersubunit rotation in active F-ATPase
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
- The proton flux through the bacterial flagellar motor.
- Direct observation of the rotation of F1-ATPase
- Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP.
- The load dependence of kinesin's mechanical cycle.
- Direct observation of kinesin stepping by optical trapping interferometry
- F 1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120 8 Steps
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