MicroScale Thermophoresis (MST) is known to be a powerful technique to quantify biomolecular interactions since it is highly sensitive to virtually any change in molecular properties. This allows for a precise quantification of molecular events independent of the size or nature of the investigated specimen. In this review, however, we give a comprehensive overview of MicroScale Thermophoresis applications that exceed the determination of equilibrium constants.
- Determine binding affinities of so far inaccessibly strong interactions with Kds in the low pM range
- Obtain additional information about binding stoichiometries, binding modes, and conformations
- Quantify Kds in complex bioliquids, even in 100 % cell lysate
- Analyze kinetics of enzyme-substrate reactions
- Detect multi-step protein unfolding processes
