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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]
Saturation binding measures the specific binding of a radioligand at varying concentrations while at equilibrium. Through this method, the number of receptors can be determined as well as affinity of the ligand to these receptors. Saturation binding experiments are often called "Scatchard experiments" as they can be graphed as a Scatchard plot ...
Scatchard analysis of radio ligand binding data from 125I-OSM binding to a variety of OSM responsive cell lines produced curvilinear graphs which the authors interpreted as the presence of two receptor species, a high affinity form with an approximate dissociation constant Kd of 1-10 pM, and a low affinity form of 0.4-1 nM. [16]
Receptor–ligand binding kinetics also involves the on- and off-rates of binding. A main goal of receptor–ligand kinetics is to determine the concentrations of the various kinetic species (i.e., the states of the receptor and ligand) at all times, from a given set of initial concentrations and a given set of rate constants.
Rotating cell‑based ligand binding assay using radioactivity or fluorescence, is a recent method that measures molecular interactions in living cells in real-time. This method allows the characterization of the binding mechanism, as well as K d, k on and k off. This principle is being applied in several studies, mainly with protein ligands ...
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.
The binding affinity is the concentration needed to occupy 50% of the sites; the lower this value is the easier it is for the ligand to occupy the binding site. The binding of the ligand to the receptor at equilibrium follows the same kinetics as an enzyme at steady-state (Michaelis–Menten equation) without the conversion of the bound ...
The GS domain of the type I receptor consists of a series of about thirty serine-glycine repeats. [7] The binding of a TGFβ family ligand causes the rotation of the receptors so that their cytoplasmic kinase domains are arranged in a catalytically favorable orientation. The Type II receptor phosphorylates serine residues of the Type I receptor ...
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