ArticleBiophysical journal1996
Small segmental rearrangements in the myosin head can explain force generation in muscle.
Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 28 citations in OpenAlex.
- Muscle active force-length curve explained by an electrophysical model of interfilament spacing.Biophysical journal · 2022Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Article
- Rigor-force producing cross-bridges in skeletal muscle fibers activated by a substoichiometric amount of ATP.Biophysical journal · 2003Article
- Axial disposition of myosin heads in isometrically contracting muscles.Biophysical journal · 2001Article
- Mechanics and models of the myosin motor.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2000Review
- The force bearing capacity of frog muscle fibres during stretch: its relation to sarcomere length and fibre width.The Journal of physiology · 1999Article
- Mechanical components of motor enzyme function.Biophysical journal · 1997Article
- Light chain-dependent myosin structural dynamics in solution investigated by transient electrical birefringence.Biophysical journal · 1997Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poisson-Boltzmann calculations of the distribution of electrostatic potentials around an actin filament in physiological-strength solutions show that negative isopotential surfaces protrude into the solvent. Each protrusion follows the actin two-start helix and is located on the sites implicated in the formation of the actomyosin complex. Molecular dynamic calculations on the S1 portion of the myosin molecule indicate that in the presence of ATP the crystallographically invisible loops (comprising residues 624-649 and 564-579) remain on the surface, whereas in the absence of ATP they can move toward the actin-binding sites and experience electrostatic forces that range from 1 to 10 pN. The molecular dynamics calculations also suggest that during the ATP cycle there exist at least three states of electrostatic interactions between the loops and actin. Every time a new interaction is formed, the strain in the myosin head increases and the energy of the complex decreases by 2kT to 5kT. This can explain muscular contraction in terms of a Huxley-Simmons-type mechanism, while requiring only rearrangements of small mobile S1 segments rather than the large shape changes in the myosin molecule postulated by the conventional tilting head model.
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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.