The Monod-Wyman-Changeux model is used to describe the saturation of hemoglobin with oxygen. Accounts for homotropic cooperative effects on each of the four binding sites.
Model number: 0239
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The Monod-Wyman-Changeux model was first used to describe indirect interactions of neighboring binding sites (each protomer of a protein has exactly one binding site) on each other (allosteric effect). It uses a simple model where the protein (Hemoglobin) can be found in one of at least two different, reversible, conformational states. The affinity for the ligand (O2) is different for the two conformational states. If a ligand binding to one site causes a confomational change of the protomer then the conformational change occurs for all protomers (binding sites). This model describes homotropic cooperative effects between binding sites but does not take into account heterotropic effects due to different allosteric ligands (ex: 3 ligands where one is an inhibitor and one is an activator for the third ligand). See Notes page for additional information.
The equations for this model may be viewed by running the JSim model applet and clicking on the Source tab at the bottom left of JSim's Run Time graphical user interface. The equations are written in JSim's Mathematical Modeling Language (MML). See the Introduction to MML and the MML Reference Manual. Additional documentation for MML can be found by using the search option at the Physiome home page.
Monod J, Wyman J, Changeux J: On the Nature of Allosteric Transitions: A Plausible Model Journal of Molecular Biology, 12:88-118, 1965
- HbO Hill slow binding
- Hb Independent
- Hb Cooperative
- Total Blood oxygen content
- Compare HbO binding models.
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[This page was last modified 02Nov16, 4:02 pm.]
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