Direct observation of kinesin stepping by optical trapping interferometry
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Summary
It is found that kinesin moves with 8-nm steps, similar to biological motors that move with regular steps.
- Type
- article
- Published
- 1993-10-21
- Cited by
- 1,817
- References
- 46
- OpenAlex
- https://openalex.org/W2152516404
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:4309346
Keywords
Optical tweezers, Kinesin, Interferometry, Molecular motor, Microtubule
References
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- Kinesin ATPase: rate-limiting ADP release.
- Tracking kinesin-driven movements with nanometre-scale precision
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- Delayed start-up of kinesin-driven microtubule gliding following inhibition by adenosine 5'-[beta,gamma-imido]triphosphate.
- The loose coupling mechanism in molecular machines of living cells.
- Selected Papers on Noise and Stochastic Processes
- Sub-piconewton force fluctuations of actomyosin in vitro
- Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle
- Decoration of the microtubule surface by one kinesin head per tubulin heterodimer
- Bovine brain kinesin is a microtubule-activated ATPase.
- Compliance of bacterial flagella measured with optical tweezers
- Motor molecules in motion
- Evidence that the head of kinesin is sufficient for force generation and motility in vitro.
- High-frequency vibration in flagellar axonemes with amplitudes reflecting the size of tubulin
Cited by
- Aspergillus nidulans apsA (anucleate primary sterigmata) encodes a coiled-coil protein required for nuclear positioning and completion of asexual development
- Toward understanding the structure and interactions of microtubules and motor proteins
- Quantitative measurements of force and displacement using an optical trap.
- Translation step size measured in single sarcomeres and single filament pairs.
- Orientation dependence of displacements by a single one-headed myosin relative to the actin filament.
- The conformational cycle of kinesin.
- An integrated laser trap/flow control video microscope for the study of single biomolecules.
- Forces required of kinesin during processive transport through cytoplasm.
- Linear and rotary molecular motors.
- All-optical constant-force laser tweezers.
- Optical trap stiffness in the presence and absence of spherical aberrations.
- Single-molecule studies of complex systems: the replisome.
- Construction and calibration of an optical trap on a fluorescence optical microscope
- Motion of microgels in electric fields.
- Mechanical properties of viruses.
- The mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A
- Kinesin walks the line: single motors observed by atomic force microscopy.
- Velocity-dependent actomyosin ATPase cycle revealed by in vitro motility assay with kinetic analysis.
- Single-molecule imaging and manipulation of biomolecular machines and systems.
- Application of the sequential n-step kinetic mechanism to polypeptide translocases.
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