Biophysics and Biomolecular Interactions Centre
Determining protein activity, stability and biophysical properties as well as 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 all these facets.
We can use the automated Multi-angle Light Scattering (MALS) in line with Size-Exclusion Chromatography (SEC)to determine the molecular mass and size of macromolecular complexes. Instruments employing optical measurements including absorbance, fluorescence, and circular dichroism (CD) can provide important insights into protein structure, stability and activity.Differential scanning calorimetry (DSC)provides detailed quantitative measure of protein stability.
Standard tools such as Isothermal Titration Calorimetry (ITC) and the newest technology of 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. Furthermore, the on rate and off rate of two molecules that interact can be measured by Surface Plasmon Resonance (SPR) and Biolayer Interferometry (BLI).
Equipment
