ArticleBiophysics (Nagoya-shi, Japan)2005
Mechanism of muscle contraction based on stochastic properties of single actomyosin motors observed
Article in Biophysics (Nagoya-shi, Japan), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed.
- Landscape-Based View on the Stepping Movement of Myosin VI.The journal of physical chemistry. B · 2022Article
- Single molecule detection, thermal fluctuation and life.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- Coupling of lever arm swing and biased Brownian motion in actomyosin.PLoS computational biology · 2014Article
- Distinct Conformation of ATP Molecule in Solution and on Protein.Biophysics (Nagoya-shi, Japan) · 2013Article
- Muscle contraction mechanism based on single molecule measurements.Journal of muscle research and cell motility · 2012Article
- From single molecule fluctuations to muscle contraction: a Brownian model of A.F. Huxley's hypotheses.PloS one · 2012Article
- Article
- Load-dependent sliding direction change of a myosin head on an actin molecule and its energetic aspects: Energy borrowing model of a cross-bridge cycle.Biophysics (Nagoya-shi, Japan) · 2009Article
- Recombinant alpha-actin for specific fluorescent labeling.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2009Article
- Single molecule measurements and molecular motors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2008Review
- Statistical properties of the dichotomous noise generated in biochemical processes.Cellular & molecular biology letters · 2008Article
- Structural change and nucleotide dissociation of Myosin motor domain: dual go model simulation.Biophysical journal · 2007Article
- Nonlinear relaxation dynamics in elastic networks and design principles of molecular machines.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Cargo-binding makes a wild-type single-headed myosin-VI move processively.Biophysical journal · 2006Article
- The path to visualization of walking myosin V by high-speed atomic force microscopy.Biophysical reviewsArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously measured the process of displacement generation by a single head of muscle myosin (S1) using scanning probe nanometry. Given that the myosin head was rigidly attached to a fairly large scanning probe, it was assumed to stably interact with an underlying actin filament without diffusing away as would be the case in muscle. The myosin head has been shown to step back and forth stochastically along an actin filament with actin monomer repeats of 5.5 nm and to produce a net movement in the forward direction. The myosin head underwent 5 forward steps to produce a maximum displacement of 30 nm per ATP at low load (<1 pN). Here, we measured the steps over a wide range of forces up to 4 pN. The size of the steps (∼5.5 nm) did not change as the load increased whereas the number of steps per displacement and the stepping rate both decreased. The rate of the 5.5-nm steps at various force levels produced a force-velocity curve of individual actomyosin motors. The force-velocity curve from the individual myosin heads was comparable to that reported in muscle, suggesting that the fundamental mechanical properties in muscle are basically due to the intrinsic stochastic nature of individual actomyosin motors. In order to explain multiple stochastic steps, we propose a model arguing that the thermally-driven step of a myosin head is biased in the forward direction by a potential slope along the actin helical pitch resulting from steric compatibility between the binding sites of actin and a myosin head. Furthermore, computer simulations show that multiple cooperating heads undergoing stochastic steps generate a long (>60 nm) sliding distance per ATP between actin and myosin filaments, i.e., the movement is loosely coupled to the ATPase cycle as observed in muscle.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.