The interactions between proteins, nucleic acids and small molecules is at the heart of all the biochemical processes that occur in life. The Biochemistry Department houses state of the art instrumentation to analyze these interactions.


Standard tools such as Isothermal Titration Calorimetry (ITC) and the newest technology Microscale Thermophoresis (MST) gather equilibrium binding constants between molecules. In the case of ITC differences in heat signatures that are measured when two molecules interact within a confined environment. On the other hand microscale thermophoresis measures the change in diffusion rate of a molecule when it interacts with another molecule.

The on rate and off rate of two molecules that interact can be measured by Surface Plasmon Resonance (SPR) and Biolayer Interferometry (BLI).

We can use the automated Multi-angle Light Scattering (MALS) in line with size-exclusion chromatography (SEC) and/or Analytical Ultracentrifugation (AUC) to determine the molecular mass and size of macromolecular complexes.


  • Biolayer Interferometry – Octet Red Biomolecular interactions
  • Biacore X100
  • SEC-MALS –Malvern with autosampler
  • Microscale Thermophoresis
  • Gryphon nano-Dropsetter with LCP
  • Scorpion liquid handling robot (provided by Jeffrey Lee, LMP)
  • UV/Vis crystallization imaging plate hotel

Octet Red BLI

Biacore X100

Microscale thermophoresis


MaRS Center, West Tower
661 University Ave., 16th Floor
University of Toronto

Coordinator and Contact

Trevor F. Moraes

Trevor F. Moraes

MaRS Center, West Tower
661 University Ave., Rm 1613