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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. How to Make Natural Food Coloring Using Everyday Ingredients

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  4. Myosin-light-chain phosphatase - Wikipedia

    en.wikipedia.org/wiki/Myosin-light-chain_phosphatase

    Because myosin undergoes a conformational change, the muscle will stay contracted even if calcium and activated MLC kinase concentrations are brought to normal levels. The conformational change must be undone to relax the muscle. [4] When myosin phosphatase binds to myosin, it removes the phosphate group. Without the group, the myosin reverts ...

  5. Food coloring - Wikipedia

    en.wikipedia.org/wiki/Food_coloring

    A variety of food colorings, added to beakers of water. Food coloring, color additive or colorant is any dye, pigment, or substance that imparts color when it is added to food or beverages. Colorants can be supplied as liquids, powders, gels, or pastes. Food coloring is commonly used in commercial products and in domestic cooking.

  6. How to DIY your own natural food coloring

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  7. Myosin head - Wikipedia

    en.wikipedia.org/wiki/Myosin_head

    The myosin head is the part of the thick myofilament made up of myosin that acts in muscle contraction, by sliding over thin myofilaments of actin.Myosin is the major component of the thick filaments and most myosin molecules are composed of a head, neck, and tail domain; the myosin head binds to thin filamentous actin, and uses ATP hydrolysis to generate force and "walk" along the thin filament.

  8. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    The folding is driven by the non-specific hydrophobic interactions, the burial of hydrophobic residues from water, but the structure is stable only when the parts of a protein domain are locked into place by specific tertiary interactions, such as salt bridges, hydrogen bonds, and the tight packing of side chains and disulfide bonds.

  9. Category:Food colorings - Wikipedia

    en.wikipedia.org/wiki/Category:Food_colorings

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