Related Experiment Video

Updated: Jul 13, 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

A computerized approach towards the estimation of binding parameters to characterize cooperative and non-cooperative

H D Quednau, M L Rao

    International Journal of Bio-Medical Computing
    |March 1, 1985
    PubMed

    More Related Videos

    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

    Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach10:01

    Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach

    Published on: June 23, 2026

    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:
    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...
    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 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...
    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...