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  2. Protein–ligand complex - Wikipedia

    en.wikipedia.org/wiki/Protein–ligand_complex

    Molecular recognition depends on affinity and specificity. Specificity means that proteins distinguish the highly specific binding partner from less specific partners and affinity allows the specific partner with high affinity to remain bound even if there are high concentrations of less specific partners with lower affinity. [3]

  3. Binding selectivity - Wikipedia

    en.wikipedia.org/wiki/Binding_selectivity

    The specificity of a receptor is determined by its spatial geometry and the way it binds to the ligand through non-covalent interactions, such as hydrogen bonding or Van der Waals forces. [2] If a receptor can be isolated a synthetic drug can be developed either to stimulate the receptor, an agonist or to block it, an antagonist.

  4. Chemical specificity - Wikipedia

    en.wikipedia.org/wiki/Chemical_specificity

    Chemical specificity is the ability of binding site of a macromolecule (such as a protein) to bind specific ligands. The fewer ligands a protein can bind, the greater its specificity. Specificity describes the strength of binding between a given protein and ligand.

  5. Ligand (biochemistry) - Wikipedia

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

    In general, high-affinity ligand binding results from greater attractive forces between the ligand and its receptor while low-affinity ligand binding involves less attractive force. In general, high-affinity binding results in a higher occupancy of the receptor by its ligand than is the case for low-affinity binding; the residence time ...

  6. Ligand binding assay - Wikipedia

    en.wikipedia.org/wiki/Ligand_binding_assay

    A ligand binding assay (LBA) is an assay, or an analytic procedure, which relies on the binding of ligand molecules to receptors, antibodies or other macromolecules. [1] A detection method is used to determine the presence and amount of the ligand-receptor complexes formed, and this is usually determined electrochemically or through a fluorescence detection method. [2]

  7. Dissociation constant - Wikipedia

    en.wikipedia.org/wiki/Dissociation_constant

    The dissociation constant is commonly used to describe the affinity between a ligand (such as a drug) and a protein; i.e., how tightly a ligand binds to a particular protein. Ligand–protein affinities are influenced by non-covalent intermolecular interactions between the two molecules such as hydrogen bonding , electrostatic interactions ...

  8. Affinity chromatography - Wikipedia

    en.wikipedia.org/wiki/Affinity_chromatography

    Immunoaffinity media (detailed below) utilizes antigens' and antibodies' high specificity to separate; immobilized metal affinity chromatography is detailed further below and uses interactions between metal ions and proteins (usually specially tagged) to separate; nucleotide/coenzyme that works to separate dehydrogenases, kinases, and ...

  9. Sensitivity and specificity - Wikipedia

    en.wikipedia.org/wiki/Sensitivity_and_specificity

    If the true status of the condition cannot be known, sensitivity and specificity can be defined relative to a "gold standard test" which is assumed correct. For all testing, both diagnoses and screening, there is usually a trade-off between sensitivity and specificity, such that higher sensitivities will mean lower specificities and vice versa.