Measuring Molecular Interactions

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. You can measure some response proportional to complex formation at equilibrium and fit to a equilibrium constant, or you can measure binding kinetics by observing binding in real time and fitting the rate constants.

Check out the CMI Binding Simulator to model equilibrium and kinetic experiments. 

Surface Plasmon Resonance (SPR)

The Biacore T200 from Cytiva, detects Surface Plasmon Resonance, an optical technique used to measure binding kinetics and binding equilibrium.

Biacore T200

Multimode Plate Reader

Spark Multimode Plate Reader from Tecan, configured with Absorbance mode, Luminescence mode, and enhanced Fusion Optics Fluorescence mode.  

tecan spark

Biolayer Interferometry (BLI)

The Octet R8e and RED384 (RH16) instruments from Sartorius detect Biolayer Interferometry, an optical technique used to measure binding kinetics and binding equilibrium.

Octet R8e and Red384

MicroScale Thermophoresis (MST)

The Monolith NT.115pico from NanoTemper detects MicroScale Thermophoresis, movement in a temperature gradient, used to measure binding equilibrium.

Monolith NT115

Mass Photometry (MP)

The TwoMP from Refeyn for Mass Photometry is a single-particle static light scattering detector, used to measure molar mass in solution.

Refeyn TwoMP

CMI Technologies to Measure Binding

 

technology comparison table - interactions

 

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