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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Cell mechanics and mechanotransduction: pathways, probes, and physiology
TL;DR: The physical bases underlying the mechanotransduction process are reviewed, techniques used to apply controlled mechanical stresses on living cells and tissues to probe mechanotranduction are discussed, and some of the important lessons that are learning from mechanical stimulation of cells with precisely controlled forces are learned.
Journal ArticleDOI
Single-molecule chemistry
TL;DR: The scanning tunneling microscope (STM) as discussed by the authors is a state-of-the-art system for direct visualization of chemistry by revealing the fundamental properties of atoms and molecules and their interactions with each other and the environment.
Journal ArticleDOI
A single myosin head moves along an actin filament with regular steps of 5.3 nanometres
TL;DR: A new instrument is developed with which individual myosin subfragment-1 molecules are captured and directly manipulated using a scanning probe to resolve the individual mechanical events of force generation by actomyosin.
Journal ArticleDOI
Reverse engineering of the giant muscle protein titin
Hongbin Li,Wolfgang A. Linke,Andres F. Oberhauser,Mariano Carrión-Vázquez,Jason Kerkvliet,Hui Lu,Piotr E. Marszalek,Julio M. Fernandez +7 more
TL;DR: This work uses protein engineering and single-molecule atomic force microscopy to examine the mechanical components that form the elastic region of human cardiac titin and shows the functional reconstitution of a protein from the sum of its parts.
Journal ArticleDOI
Molecular motors: structural adaptations to cellular functions
TL;DR: Differences in duty ratio can explain the diversity of structures, speeds and oligomerization states of members of the large kinesin, myosin and dynein families of motors.
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.
Journal ArticleDOI
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.