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  2. Myosin - Wikipedia

    en.wikipedia.org/wiki/Myosin

    Myosin X is an unconventional myosin motor, which is functional as a dimer. The dimerization of myosin X is thought to be antiparallel. [53] This behavior has not been observed in other myosins. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments.

  3. Motor protein - Wikipedia

    en.wikipedia.org/wiki/Motor_protein

    Myosin II is an elongated protein that is formed from two heavy chains with motor heads and two light chains. Each myosin head contains actin and ATP binding site. The myosin heads bind and hydrolyze ATP, which provides the energy to walk toward the plus end of an actin filament. Myosin II are also vital in the process of cell division. For ...

  4. Composition of the human body - Wikipedia

    en.wikipedia.org/wiki/Composition_of_the_human_body

    Pie charts of typical human body composition by percent of mass, and by percent of atomic composition (atomic percent) Body composition may be analyzed in various ways. This can be done in terms of the chemical elements present, or by molecular structure e.g., water , protein , fats (or lipids ), hydroxyapatite (in bones), carbohydrates (such ...

  5. Muscle - Wikipedia

    en.wikipedia.org/wiki/Muscle

    Muscle tissue contains special contractile proteins called actin and myosin which interact to cause movement. Among many other muscle proteins, present are two regulatory proteins, troponin and tropomyosin. [1] Muscle tissue varies with function and location in the body. In vertebrates, the three types are: skeletal, cardiac (both striated), and

  6. Adenosine triphosphate - Wikipedia

    en.wikipedia.org/wiki/Adenosine_triphosphate

    ATP is initially bound to myosin. When ATPase hydrolyzes the bound ATP into ADP and inorganic phosphate, myosin is positioned in a way that it can bind to actin. Myosin bound by ADP and P i forms cross-bridges with actin and the subsequent release of ADP and P i releases energy as the power stroke. The power stroke causes actin filament to ...

  7. MYO1C - Wikipedia

    en.wikipedia.org/wiki/MYO1C

    Myosin-Ic is a protein that in humans is encoded by the MYO1C gene. [5] [6] This gene encodes a member of the unconventional myosin protein family, which are actin-based molecular motors. The protein is found in the cytoplasm, and one isoform with a unique N-terminus is also found in the nucleus.

  8. MYH1 - Wikipedia

    en.wikipedia.org/wiki/MYH1

    Myosin-1, also known as 'striated muscle myosin heavy chain 1', is a protein that in humans is encoded by the MYH1 gene. [5] [6] This gene is most highly expressed in fast type IIX/D muscle fibres of vertebrates and encodes a protein found uniquely in striated muscle; it is a class II myosin with a long coiled coil tail that dimerizes and should not be confused with 'Myosin 1' encoded by the ...

  9. Tropomyosin - Wikipedia

    en.wikipedia.org/wiki/Tropomyosin

    Myosin belongs to a family of motor proteins, and the muscle isoforms of this family comprise the thick filament. The thin filament is made of the skeletal muscle isoforms of actin. Each myosin protein 'paddles' along the thin actin filament, repeatedly binding to myosin-binding sites along the actin filament, ratcheting and letting go.