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  2. Dissociation constant - Wikipedia

    en.wikipedia.org/wiki/Dissociation_constant

    In chemistry, biochemistry, and pharmacology, a dissociation constant (K D) is a specific type of equilibrium constant that measures the propensity of a larger object to separate (dissociate) reversibly into smaller components, as when a complex falls apart into its component molecules, or when a salt splits up into its component ions.

  3. Electrophoretic mobility shift assay - Wikipedia

    en.wikipedia.org/wiki/Electrophoretic_mobility...

    Unless the complex is very long lived under gel conditions, or dissociation during electrophoresis is taken into account, the number derived is an apparent Kd. If the protein concentration is not known but the complex stoichiometry is, the protein concentration can be determined by increasing the concentration of DNA probe until further ...

  4. Hill equation (biochemistry) - Wikipedia

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

    The Hill equation is used extensively in pharmacology to quantify the functional parameters of a drug [citation needed] and are also used in other areas of biochemistry. The Hill equation can be used to describe dose-response relationships, for example ion channel open-probability (P-open) vs. ligand concentration.

  5. Tryptophan 2,3-dioxygenase - Wikipedia

    en.wikipedia.org/wiki/Tryptophan_2,3-dioxygenase

    56720 Ensembl ENSG00000262635 ENSG00000151790 ENSMUSG00000028011 UniProt P48775 P48776 RefSeq (mRNA) NM_005651 NM_019911 RefSeq (protein) NP_005642 NP_064295 Location (UCSC) Chr 4: 155.85 – 155.92 Mb Chr 3: 81.86 – 81.88 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse In enzymology, tryptophan 2,3-dioxygenase (EC 1.13.11.11) is a heme enzyme that catalyzes the oxidation of L ...

  6. Binding constant - Wikipedia

    en.wikipedia.org/wiki/Binding_constant

    The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant K, [1] and is the inverse of the dissociation constant. [2] It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as:

  7. Dissociation rate - Wikipedia

    en.wikipedia.org/wiki/Dissociation_rate

    The dissociation rate in chemistry, biochemistry, and pharmacology is the rate or speed at which a ligand dissociates from a protein, for instance, a receptor. [1] It is an important factor in the binding affinity and intrinsic activity (efficacy) of a ligand at a receptor. [1]

  8. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    Combining with other new techniques, this method can be used to screen protein–protein interactions and their modulators, [3] DERB. [4] Affinity electrophoresis as used for estimation of binding constants, as for instance in lectin affinity electrophoresis or characterization of molecules with specific features like glycan content or ligand ...

  9. 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]