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  2. Protein quaternary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_quaternary_structure

    The G-protein coupled receptor pathway involves a heterotrimeric protein known as a G-protein. G-proteins contain three distinct subunits known as the G-alpha, G-beta, and G-gamma subunits. When the G-protein is activated, it binds to the G-protein coupled receptor protein and the cell signaling pathway is initiated.

  3. Biomolecular structure - Wikipedia

    en.wikipedia.org/wiki/Biomolecular_structure

    Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits.

  4. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein structures range in size from tens to several thousand amino acids. [2] By physical size, proteins are classified as nanoparticles, between 1–100 nm. Very large protein complexes can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament.

  5. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    This protein was the first to have its structure solved by X-ray crystallography by Max Perutz and Sir John Cowdery Kendrew in 1958, for which they received a Nobel Prize in Chemistry. A biomolecule or biological molecule is loosely defined as a molecule produced by a living organism and essential to one or more typically biological processes. [1]

  6. File:Levels of structural organization of a protein.svg

    en.wikipedia.org/wiki/File:Levels_of_structural...

    English: Functional proteins have four levels of structural organization: 1) Primary Structure : the linear structure of amino acids in the polypeptide chain 2) Secondary Structure : hydrogen bonds between peptide group chains in an alpha helix or beta 3) Tertiary Structure : three-dimensional structure of alpha helixes and beta helixes folded

  7. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    The structure of a protein, such as an enzyme, may change upon binding of its natural ligands, for example a cofactor. In this case, the structure of the protein bound to the ligand is known as holo structure, while the unbound protein has an apo structure. [8]

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  9. Myosin - Wikipedia

    en.wikipedia.org/wiki/Myosin

    Myosins (/ ˈ m aɪ ə s ɪ n,-oʊ-/ [1] [2]) are a family of motor proteins (though most often protein complexes) best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes. They are ATP-dependent and responsible for actin-based motility. The first myosin (M2) to be discovered was in 1864 by ...