ArticleBiophysical journal2001
Hidden-Markov methods for the analysis of single-molecule actomyosin displacement data: the variance-Hidden-Markov method.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed.
- Single-Molecule Investigation of Load-Dependent Actomyosin Dissociation Kinetics for Cardiac and Slow Skeletal Myosin.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Modeling thick filament activation suggests a molecular basis for force depression.Biophysical journal · 2024Article
- A mutation in switch I alters the load-dependent kinetics of myosin Va.Nature communications · 2023Article
- Cardiac ventricular myosin and slow skeletal myosin exhibit dissimilar chemomechanical properties despite bearing the same myosin heavy chain isoform.The Journal of biological chemistry · 2022Article
- Generalizing HMMs to Continuous Time for Fast Kinetics: Hidden Markov Jump Processes.Biophysical journal · 2021Article
- Computational Tool for Ensemble Averaging of Single-Molecule Data.Biophysical journal · 2021Article
- FRET and optical trapping reveal mechanisms of actin activation of the power stroke and phosphate release in myosin V.The Journal of biological chemistry · 2020Article
- Single-molecule analysis reveals that regulatory light chains fine-tune skeletal myosin II function.The Journal of biological chemistry · 2020Article
- Step Sizes and Rate Constants of Single-headed Cytoplasmic Dynein Measured with Optical Tweezers.Scientific reports · 2018Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Working stroke of the kinesin-14, ncd, comprises two substeps of different direction.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Interrogating biology with force: single molecule high-resolution measurements with optical tweezers.Biophysical journal · 2013Review
- Mechanical and kinetic properties of β-cardiac/slow skeletal muscle myosin.Journal of muscle research and cell motility · 2012Article
- Ultrafast force-clamp spectroscopy of single molecules reveals load dependence of myosin working stroke.Nature methods · 2012Article
- Moving into the cell: single-molecule studies of molecular motors in complex environments.Nature reviews. Molecular cell biology · 2011Review
- A hidden Markov model for single particle tracks quantifies dynamic interactions between LFA-1 and the actin cytoskeleton.PLoS computational biology · 2009Article
- Hidden markov analysis of short single molecule intensity trajectories.The journal of physical chemistry. B · 2009Article
- Extracting kinetics information from single-molecule fluorescence resonance energy transfer data using hidden markov models.The journal of physical chemistry. B · 2009Article
- Multiple objects tracking in fluorescence microscopy.Journal of mathematical biology · 2009Article
- Single-molecule measurement of the stiffness of the rigor myosin head.Biophysical journal · 2008Article
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4 authors.
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Abstract
In single-molecule experiments on the interaction between myosin and actin, mechanical events are embedded in Brownian noise. Methods of detecting events have progressed from simple manual detection of shifts in the position record to threshold-based selection of intermittent periods of reduction in noise. However, none of these methods provides a "best fit" to the data. We have developed a Hidden-Markov algorithm that assumes a simple kinetic model for the actin-myosin interaction and provides automatic, threshold-free, maximum-likelihood detection of events. The method is developed for the case of a weakly trapped actin-bead dumbbell interacting with a stationary myosin molecule (Finer, J. T., R. M. Simmons, and J. A. Spudich. 1994. Nature. 368:113-119). The algorithm operates on the variance of bead position signals in a running window, and is tested using Monte Carlo simulations to formulate ways of determining the optimum window width. The working stroke is derived and corrected for actin-bead link compliance. With experimental data, we find that modulation of myosin binding by the helical structure of the actin filament complicates the determination of the working stroke; however, under conditions that produce a Gaussian distribution of bound levels (cf. Molloy, J. E., J. E. Burns, J. Kendrick-Jones, R. T. Tregear, and D. C. S. White. 1995. Nature. 378:209-212), four experiments gave working strokes in the range 5.4-6.3 nm for rabbit skeletal muscle myosin S1.
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