ArticleJournal of molecular biology2014
Flexibility within the heads of muscle myosin-2 molecules.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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.
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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.
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Who cites it
12 citing papers in PubMed.
- Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022Article
- Myosin II Filament Dynamics in Actin Networks Revealed with Interferometric Scattering Microscopy.Biophysical journal · 2020Article
- Dilated cardiomyopathy mutation in the converter domain of human cardiac myosin alters motor activity and response to omecamtiv mecarbil.The Journal of biological chemistry · 2019Article
- Nonlinear Actomyosin Elasticity in Muscle?Biophysical journal · 2019Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Effect of Passive, Active and Combined Warm up on Lower Limb Muscle Performance and Dynamic Stability in Recreational Sports Players.Journal of clinical and diagnostic research : JCDR · 2017Article
- Difference in the hydration water mobility around F-actin and myosin subfragment-1 studied by quasielastic neutron scattering.Biochemistry and biophysics reports · 2016Article
- Force per cross-sectional area from molecules to muscles: a general property of biological motors.Royal Society open science · 2016Article
- Direct observation shows superposition and large scale flexibility within cytoplasmic dynein motors moving along microtubules.Nature communications · 2015Article
- Article
- The contributions of filaments and cross-bridges to sarcomere compliance in skeletal muscle.The Journal of physiology · 2014Article
- The path to visualization of walking myosin V by high-speed atomic force microscopy.Biophysical reviewsArticle
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
We show that negative-stain electron microscopy and image processing of nucleotide-free (apo) striated muscle myosin-2 subfragment-1 (S1), possessing one light chain or both light chains, is capable of resolving significant amounts of structural detail. The overall appearance of the motor and the lever is similar in rabbit, scallop and chicken S1. Projection matching of class averages of the different S1 types to projection views of two different crystal structures of apo S1 shows that all types most commonly closely resemble the appearance of the scallop S1 structure rather than the methylated chicken S1 structure. Methylation of chicken S1 has no effect on the structure of the molecule at this resolution: it too resembles the scallop S1 crystal structure. The lever is found to vary in its angle of attachment to the motor domain, with a hinge point located in the so-called pliant region between the converter and the essential light chain. The chicken S1 crystal structure lies near one end of the range of flexion observed. The Gaussian spread of angles of flexion suggests that flexibility is driven thermally, from which a torsional spring constant of ~23 pN·nm/rad² is estimated on average for all S1 types, similar to myosin-5. This translates to apparent cantilever-type stiffness at the tip of the lever of 0.37 pN/nm. Because this stiffness is lower than recent estimates from myosin-2 heads attached to actin, we suggest that binding to actin leads to an allosteric stiffening of the motor-lever junction.
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Registered trials
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