Our facility offers powerful analytical instrumentation used to study macromolecular interactions.
We have instrumentation ideal for acquiring high quality kinetic, affinity and thermodynamic data for biomolecular interactions.
Our facility enables you to achieve direct, label-free measurement of binding affinity and thermodynamics of biomolecules in a single experiment.
Surface plasmon resonance (SPR) is an optical technique for measuring macromolecular interactions in real time. It does not require modification of binding partners, and it provides detailed information about on- and off-rates, as well as stoichiometry.
Isothermal titration calorimetry (ITC) — a technique used in quantitative studies of a wide variety of biomolecular interactions — requires no modification of binding partners, either with fluorescent tags or through immobilization. It measures the affinity of binding partners in their native states, including ligand binding to live cells or to ligand binding sites incorporated into synthetic vesicles or particles.
404 Biomedical Research Building
656 Biomedical Research Building