Journal ArticleDOI
Single myosin molecule mechanics: piconewton forces and nanometre steps
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TLDR
A new in vitro assay using a feedback enhanced laser trap system allows direct measurement of force and displacement that results from the interaction of a single myosin molecule with a single suspended actin filament.Abstract:
A new in vitro assay using a feedback enhanced laser trap system allows direct measurement of force and displacement that results from the interaction of a single myosin molecule with a single suspended actin filament. Discrete stepwise movements averaging 11 nm were seen under conditions of low load, and single force transients averaging 3-4 pN were measured under isometric conditions. The magnitudes of the single forces and displacements are consistent with predictions of the conventional swinging-crossbridge model of muscle contraction.read more
Citations
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Vinculin anchors contractile actin to the cardiomyocyte adherens junction.
TL;DR: This work shows that force-responsive cardiomyocyte AJs recruit actin-binding ligands to selectively couple actin networks and identifies vinculin as a critical link to contractile actomyosin and offers insight to how actin integration at the AJ is regulated to provide stability under mechanical load.
Journal ArticleDOI
Investigations of Molecular Mechanisms of Actin–Myosin Interactions in Cardiac Muscle
TL;DR: Using the optical trap and the in vitro motility assay, functional characteristics of the cardiac myosin isoforms, molecular mechanisms of the calcium-dependent regulation of actin–myosin interaction, and the role of myos in and tropomyosinisoforms in the cooperativity mechanisms in myocardium are studied.
Journal ArticleDOI
Motors and their tethers: the role of secondary binding sites in processive motility.
TL;DR: Many of the processive motors have now been found to utilize secondary binding sites that aid in motor processivity.
Posted Content
A cycling state that can lead to glassy dynamics in intracellular transport
Monika Scholz,Stanislav Burov,Kimberly L. Weirich,Bjorn Scholz,S. M. Ali Tabei,Margaret L. Gardel,Aaron R. Dinner +6 more
TL;DR: It is demonstrated that trends in the dynamics with the motor valency exist in individual trajectories of myosin II on an actin network, and how cells could regulate intracellular transport and, in turn, biological function, by controlling their cytoskeletal network structures locally is discussed.
References
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Journal ArticleDOI
Proposed Mechanism of Force Generation in Striated Muscle
A. F. Huxley,R. M. Simmons +1 more
TL;DR: Recordings of the change in tension in striated muscle after a sudden alteration of the length have made it possible to suggest how the force between the thick and thin muscle filaments may be generated.
Journal ArticleDOI
Three-dimensional structure of myosin subfragment-1: a molecular motor
Ivan Rayment,Wojciech Rypniewski,Karen Schmidt-Bäse,Karen Schmidt-Bäse,Robert Smith,Diana R. Tomchick,Diana R. Tomchick,Matthew M. Benning,Donald A. Winkelmann,Gary E. Wesenberg,Hazel M. Holden +10 more
TL;DR: The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described, and this structure of a molecular motor was determined by single crystal x-ray diffraction.
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Direct observation of kinesin stepping by optical trapping interferometry
TL;DR: It is found that kinesin moves with 8-nm steps, similar to biological motors that move with regular steps.
Journal ArticleDOI
The Mechanism of Muscular Contraction
TL;DR: There is now a real possibility of solving the problem in complete detail, provided a way can be found to crystallize a recently purified globular subfragment of the myosin molecule, and some apparently paradoxical properties of the system are revealed.
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Bead movement by single kinesin molecules studied with optical tweezers
TL;DR: The results of this study are consistent with a model in which kinesin detaches briefly from the microtubule during a part of each mechanochemical cycle, rather than a models in whichKinesin remains bound at all times.