Allosteric Binding Calculator
The Allosteric Binding Calculator is a free, scientifically accurate online tool designed for biochemists, pharmacologists, and students to calculate ligand binding parameters in allosteric proteins using established models such as the Monod-Wyman-Changeux (MWC) concerted model and the Adair-Klotz sequential model.
Calculate Allosteric Parameters
About the Allosteric Binding Calculator
The Allosteric Binding Calculator is a powerful, research-grade online tool that enables precise computation of ligand binding to allosteric proteins. Allostery, first conceptualized by Monod and Jacob in 1961 and rigorously modeled by Monod, Wyman, and Changeux (MWC) in 1965, remains one of the most important regulatory mechanisms in biology.
What is Allosteric Binding?
Allosteric binding occurs when a ligand binds to a site distinct from the active site (allosteric site), inducing a conformational change that alters the affinity of the active site for its substrate or ligand. This phenomenon is central to oxygen binding in hemoglobin, enzyme regulation, G-protein-coupled receptors (GPCRs), and many drug targets. You can read more on Allosteric Binding.
Scientific Models Used
This calculator implements two gold-standard models:
- Monod-Wyman-Changeux (MWC) Concerted Model – Assumes all subunits switch together between Tense (T) and Relaxed (R) states.
- Adair-Klotz Sequential Model – Allows progressive change in affinity as each ligand binds (K1, K2, K3…).
Key Parameters Calculated
- Fractional Saturation (Y): Y = bound sites / total sites
- Hill Coefficient (nH): Measure of cooperativity (nH > 1 = positive; nH < 1 = negative)
- Kd₅₀: Ligand concentration at 50% saturation
- Cooperativity classification
Why Use This Allosteric Binding Calculator?
In drug discovery, 30–40% of current therapeutics target allosteric sites because they offer higher selectivity and fewer side effects. Accurate modeling of allosteric behavior is essential for rational drug design, understanding enzyme kinetics, and interpreting oxygen dissociation curves.
When to Use This Tool
- Analyzing hemoglobin/myoglobin oxygen binding data
- Characterizing cooperative enzymes (e.g., phosphofructokinase)
- Studying GPCR allosteric modulators
- Teaching biochemistry and pharmacology courses
- Screening allosteric drug candidates in silico
How to Use – Step by Step
- Enter the number of binding sites (e.g., 4 for hemoglobin)
- Input ligand concentration and dissociation constants
- For MWC: provide Kd(R), Kd(T), and the allosteric constant L₀
- Click “Calculate Binding”
- Interpret the Hill coefficient and saturation curve behavior
This tool is built with peer-reviewed equations published in Journal of Molecular Biology (1965) and Advances in Protein Chemistry. All calculations are performed client-side for speed and privacy.
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References & Further Reading
- Monod, J., Wyman, J., & Changeux, J. P. (1965). On the nature of allosteric transitions. Journal of Molecular Biology.
- Koshland, D. E., et al. (1966). Comparison of experimental binding data and theoretical models in proteins containing subunits.
- Changeux, J. P. (2012). Allostery and the Monod-Wyman-Changeux model. Journal of Molecular Biology.
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