ArticleProceedings of the National Academy of Sciences of the United States of America1994
Fluctuation analysis of motor protein movement and single enzyme kinetics.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
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Who cites it
96 citing papers in PubMed.
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- Physical Forces Determining the Persistency and Centering Precision of Microtubule Asters.Nature physics · 2018Article
- Particle Manipulation by Optical Forces in Microfluidic Devices.Micromachines · 2018Review
- Full molecular trajectories of RNA polymerase at single base-pair resolution.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A Multi-stage Representation of Cell Proliferation as a Markov Process.Bulletin of mathematical biology · 2017Article
- Statistical Measures to Quantify Similarity between Molecular Dynamics Simulation Trajectories.Entropy (Basel, Switzerland) · 2017Article
- Visible/near-infrared subdiffraction imaging reveals the stochastic nature of DNA walkers.Science advances · 2017Article
- Cargo Transport by Two Coupled Myosin Va Motors on Actin Filaments and Bundles.Biophysical journal · 2016Article
- The Kinesin-5 Chemomechanical Cycle Is Dominated by a Two-heads-bound State.The Journal of biological chemistry · 2016Article
- The Kinesin-1 Chemomechanical Cycle: Stepping Toward a Consensus.Biophysical journal · 2016Review
- Effects of Obstacles on the Dynamics of Kinesins, Including Velocity and Run Length, Predicted by a Model of Two Dimensional Motion.PloS one · 2016Article
- Interrogating the activities of conformational deformed enzyme by single-molecule fluorescence-magnetic tweezers microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
36 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We studied fluctuations in the displacement of silica beads driven by single molecules of the motor protein kinesin, moving under low mechanical loads at saturating ATP concentrations. The variance in position was significantly smaller than expected for the case of stepwise movement along a regular lattice of positions with exponentially distributed intervals. The small variance suggests that two or more sequential processes with comparable reaction rates dominate the biochemical cycle. The low value is inconsistent with certain recently proposed thermal ratchet models for motor movement as well as with scenarios where the hydrolysis of a single ATP molecule leads to a cluster of several steps. Fluctuation analysis is a potential powerful tool for studying kinetic behavior whenever the output of a single enzyme can be monitored.
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