Isothermal Titration Calorimetry

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Measuring Molecular Interactions

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A wide array of biomolecular interactions from protein/protein interactions to small molecule ligand/compound binding interactions are important in biology. Fundamentally, there are two ways to measure (or quantify) binding of any of these interactions...

I want to measure a Kd, how do I choose which technique is best?

FAQ

The CMI has four primary technologies to quantify molecular interactions: Surface Plasmon Resonance (SPR) and Biolayer Interferometry (BLI), Isothermal Titration Calorimetry (ITC) and MicroScale Thermophoresis (MST). Each technologies has its advantages...

To measure a molecular interaction, how do you choose which molecule to be kept at a fixed concentration and which to vary in concentration?

FAQ

The choice of which molecule to keep constant and which to vary will depend on the experiment type, the properties of the molecules and the stoichiometry of the interaction.

For ITC, where neither protein is labeled or immobilized, either molecule can be...

Isothermal Titration Calorimetry (ITC)

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The MicroCal ITC200 from Malvern detects enthalpy of binding for Isothermal Titration Calorimetry, used to measure binding equilibrium.