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Related Concept Videos

Actin and Myosin in Muscle Contraction01:16

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Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
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Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well...
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Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
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Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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Power motivation and achievement motivation are two essential social motives identified by psychologist David McClelland. These motives influence behavior in various personal and professional contexts, shaping how individuals interact with others and pursue their goals.
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Total voids in concrete encompass gel water volume, capillary pores, and entrapped air. Gel water (retained within the cement hydration products) and physically entrapped or adsorbed water are significant for the hydration process. For complete hydration, it's estimated that the space needed for the products of a cubic centimeter of cement doubles. Capillary pores constitute the unoccupied space within the hydrated cement paste, with their size largely influenced by the water-to-cement...
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Related Experiment Video

Updated: Jan 21, 2026

Author Spotlight: Unraveling the Role of Myosin-7a and Usher Proteins in Hearing and Human Disease
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How myosin II achieves total shutdown.

Ben Short

    The Journal of General Physiology
    |August 10, 2019
    PubMed
    Summary

    Researchers revealed the 3-D structure of the 10S myosin II motor protein. Key interactions between its head and tail domains were identified, explaining how the protein remains inactive.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Structural Biology

    Background:

    • Myosin II is a crucial motor protein involved in various cellular processes.
    • Understanding the regulation of myosin II activity is essential for comprehending cell motility and function.
    • The 10S conformation represents a key regulatory state of myosin II.

    Purpose of the Study:

    • To elucidate the three-dimensional structure of the 10S form of myosin II.
    • To identify the specific molecular interactions responsible for maintaining myosin II in its inactive state.

    Main Methods:

    • X-ray crystallography was employed to determine the high-resolution 3D structure.
    • Biochemical assays were used to validate the functional implications of the observed interactions.

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    Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
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    Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
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    Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
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    Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy

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    Main Results:

    • The study successfully resolved the 3D structure of the 10S myosin II.
    • Key intramolecular interactions between the myosin head and tail domains were identified.
    • These interactions were shown to stabilize the protein in a conformation that prevents motor activity.

    Conclusions:

    • The determined structure provides a molecular basis for the regulation of myosin II activity.
    • This finding offers insights into the mechanism of motor protein inactivation.
    • The results pave the way for understanding how myosin II is switched on and off in cellular contexts.