Related Experiment Video

Updated: Aug 5, 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

The effect of hemoglobin ligands on the kinetics of human hemoglobin A1c formation

C H Lowrey, S J Lyness, J S Soeldner

    The Journal of Biological Chemistry
    |September 25, 1985
    PubMed

    More Related Videos

    Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry08:23

    Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry

    Published on: November 5, 2019

    Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance10:07

    Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

    Published on: August 26, 2025

    Related Concept Videos

    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...
    Hemoglobin01:24

    Hemoglobin

    Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
    When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
    Oxygen Transport in the Blood01:27

    Oxygen Transport in the Blood

    Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
    Factors Affecting Protein-Drug Binding: Drug-Related Factors01:18

    Factors Affecting Protein-Drug Binding: Drug-Related Factors

    Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
    One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In contrast,...
    Factors Affecting Protein-Drug Binding: Patient-Related Factors01:29

    Factors Affecting Protein-Drug Binding: Patient-Related Factors

    Protein-drug binding, a pivotal aspect of pharmacokinetics, is subject to considerable variability influenced by an array of patient-related factors. The intricate interplay of age, individual differences, and pathological conditions significantly impact the binding dynamics and subsequent pharmacological effects.
    Age stands as a key determinant in protein-drug binding. Neonates, characterized by low albumin content, experience heightened concentrations of unbound drugs such as phenytoin and...