The IBBR houses standard volume isothermal titration calorimeter (ITC) and differential scanning calorimeter (DSC) instruments that provide precise measures of the affinity, and associated thermodynamic parameters, of biomolecular interactions and the stability, and associated thermodynamic parameters, of biomolecules in solution, respectively.
The IBBR houses a number of mass spectrometers, including an HDX-MS system, that allow measurement of the sequence, post-translational modifications (PTMs) and structure of biological molecules, complexes formed by these molecules and heterogeneous mixtures of these molecules in solution.
Our researchers have expertise in the characterization of the proteins including stability, structure/dynamic properties, size, covalent modification (i.e. phosphorylation, ubiquitination, methylation, glycosylation etc). Services for the identification of unknown proteins are available using a multitude of biophysical/biochemical techniques including denaturing polyacrylamide gel electrophoresis (SDS-PAGE), FPLC, mass spectrometry (MS), isothermal titration calorimetry (ITC), nuclear magnetic resonance (NMR), differential scanning calorimetry (DSC), circular dichroism (CD), fluorescence, UV/Vis, DLS, analytical ultracentrifugation (AUC), kinetic stop-flow/quench-flow, and surface plasmon resonance (SPR) techniques. Expertise & equipment for measuring enzyme kinetics, binding kinetics, and thermodynamic properties of a enzyme/proteins are also available including monitoring binding to substrates, other proteins, ligands, and/or oligomerization properties.