Microscale Thermophoresis (MST) detects changes in the hydration shell of molecules and measures biomolecular interactions under close to native conditions. Technology uses infrared-lasers to create precise microscale temperature gradient within glass capillaries and molecules move along these temperature gradients. When molecules bind or dissociate, the change in their primary, secondary, tertiary and/or quaternary structure changes the hydration shell of the biomolecule and affects the thermophoretic movement. This movement is used to determine binding from single metal ions to the formation of protein complexes with a dynamic range from mM to pM affinities.
Possible MST applications are:
- Protein-Nucleic Acid
- Nucleic Acid-Nucleic Acid
- Ribosome-Protein, Ribosome-Small molecule
- Protein modifications as phosphorylation