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  2. Adenosine triphosphate - Wikipedia

    en.wikipedia.org/wiki/Adenosine_triphosphate

    Interactive animation of the structure of ATP. Adenosine triphosphate (ATP) is a nucleoside triphosphate [2] that provides energy to drive and support many processes in living cells, such as muscle contraction, nerve impulse propagation, and chemical synthesis.

  3. ATP hydrolysis - Wikipedia

    en.wikipedia.org/wiki/ATP_hydrolysis

    Structure of ATP Structure of ADP Four possible resonance structures for inorganic phosphate. ATP hydrolysis is the catabolic reaction process by which chemical energy that has been stored in the high-energy phosphoanhydride bonds in adenosine triphosphate (ATP) is released after splitting these bonds, for example in muscles, by producing work in the form of mechanical energy.

  4. Nucleoside triphosphate - Wikipedia

    en.wikipedia.org/wiki/Nucleoside_triphosphate

    Nucleoside triphosphates cannot easily cross the cell membrane, so they are typically synthesized within the cell. [5] Synthesis pathways differ depending on the specific nucleoside triphosphate being made, but given the many important roles of nucleoside triphosphates, synthesis is tightly regulated in all cases. [ 6 ]

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  6. File:ATP structure.svg - Wikipedia

    en.wikipedia.org/wiki/File:ATP_structure.svg

    Derivative works of this file: ATP structure revised.png: SVG development . The SVG code is . This structural formula was created with Inkscape. The ...

  7. Phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Phosphorylation

    Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the "high-energy" exchange medium in the cell. During aerobic respiration, ATP is synthesized in the mitochondrion by addition of a third phosphate group to adenosine diphosphate (ADP) in a ...

  8. ATP synthase - Wikipedia

    en.wikipedia.org/wiki/ATP_synthase

    The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy (cryo-EM) studies of the complex. The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps around the complex as it joins F 1 to F O.

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