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MicroScale Thermophoresis: More than binding affinities

1 min read
Mar 24, 2014

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