Related Experiment Video

Updated: Oct 6, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
13:26

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

Investigation of the competition of two ligands for the same binding sites on a protein

N Lecureuil, J Trochet, L Garreau

    Analytical Biochemistry
    |December 1, 1986
    PubMed

    More Related Videos

    Comparing the Affinity of GTPase-binding Proteins using Competition Assays10:37

    Comparing the Affinity of GTPase-binding Proteins using Competition Assays

    Published on: October 8, 2015

    An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions08:40

    An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

    Published on: March 14, 2016

    Related Concept Videos

    Ligand Binding Sites02:40

    Ligand Binding Sites

    Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
    Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
    The Equilibrium Binding Constant and Binding Strength02:18

    The Equilibrium Binding Constant and Binding Strength

    The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
    Ligand Binding and Linkage00:49

    Ligand Binding and Linkage

    Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
    Cooperative Allosteric Transitions01:58

    Cooperative Allosteric Transitions

    Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
    Ligand Binding and Linkage00:49

    Ligand Binding and Linkage

    Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
    Ligand Binding Sites02:40

    Ligand Binding Sites

    Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
    Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...