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  2. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Molecular binding occurs in biological complexes (e.g., between pairs or sets of proteins, or between a protein and a small molecule ligand it binds) and also in abiologic chemical systems, e.g. as in cases of coordination polymers and coordination networks such as metal-organic frameworks.

  3. Binding site - Wikipedia

    en.wikipedia.org/wiki/Binding_site

    At the regulatory site, the binding of a ligand may elicit amplified or inhibited protein function. [ 4 ] [ 22 ] The binding of a ligand to an allosteric site of a multimeric enzyme often induces positive cooperativity, that is the binding of one substrate induces a favorable conformation change and increases the enzyme's likelihood to bind to ...

  4. Ligand (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Ligand_(biochemistry)

    In DNA-ligand binding studies, the ligand can be a small molecule, ion, [1] or protein [2] which binds to the DNA double helix. The relationship between ligand and binding partner is a function of charge, hydrophobicity, and molecular structure. Binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and Van der Waals forces.

  5. Cooperative binding - Wikipedia

    en.wikipedia.org/wiki/Cooperative_binding

    The first description of cooperative binding to a multi-site protein was developed by A.V. Hill. [4] Drawing on observations of oxygen binding to hemoglobin and the idea that cooperativity arose from the aggregation of hemoglobin molecules, each one binding one oxygen molecule, Hill suggested a phenomenological equation that has since been named after him:

  6. Transition metal dioxygen complex - Wikipedia

    en.wikipedia.org/wiki/Transition_metal_dioxygen...

    These binding modes include μ 2-η 2,η 2-, μ 2-η 11-, and μ 2-η 1,η 2-. Depending on the degree of electron-transfer from the dimetal unit, these O 2 ligands can again be described as peroxo or superoxo. Hemocyanin is an O 2-carrier that utilizes a bridging O2 binding motif. It features a pair of copper centers. [10] Structure of [Co ...

  7. Cooperativity - Wikipedia

    en.wikipedia.org/wiki/Cooperativity

    One manifestation of this is enzymes or receptors that have multiple binding sites where the affinity of the binding sites for a ligand is apparently increased, positive cooperativity, or decreased, negative cooperativity, upon the binding of a ligand to a binding site. For example, when an oxygen atom binds to one of hemoglobin's four binding ...

  8. Cell signaling - Wikipedia

    en.wikipedia.org/wiki/Cell_signaling

    However, for many cell surface receptors, ligand-receptor interactions are not directly linked to the cell's response. The activated receptor must first interact with other proteins inside the cell before the ultimate physiological effect of the ligand on the cell's behavior is produced. Often, the behavior of a chain of several interacting ...

  9. Pi backbonding - Wikipedia

    en.wikipedia.org/wiki/Pi_backbonding

    σ bonding from electrons in CO's HOMO to metal center d-orbital. π backbonding from electrons in metal center d-orbital to CO's LUMO. The electrons are partially transferred from a d-orbital of the metal to anti-bonding molecular orbitals of CO (and its analogs). This electron-transfer strengthens the metal–C bond and weakens the C–O bond.