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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...
Including:
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...
The amount (volume and concentration) of sample that you need will vary by method and by the Kd (equilibrium dissociation constant) of the interaction. For guidelines see the CMI technology comparison table. Binding assays will typically have one...
The relative size of the molecules isn't generally the deciding factor. Large proteins will typically give larger signals, but that isn’t necessarily better.
For protein/protein interactions, start by considering other properties of the proteins. Most...
MST experiments on the Monolith NT.115 pico require that one of the binding partners is fluorescently labeled.
For protein/protein interactions, start by considering the amounts, solubility and sequence of the proteins. The labeled target is typically...
The Monolith NT.115pico from NanoTemper detects MicroScale Thermophoresis, movement in a temperature gradient, used to measure binding equilibrium.
The Octet RED384 and BLItz instruments from Sartorius detect Biolayer Interferometry, an optical technique used to measure binding kinetics and binding equilibrium.