The Protein-Protein Interactions Analysis Platform, located across multiple rooms in the Bellini Life Sciences Complex, provides state-of-the-art instrumentation for studying biomolecular interactions. Whether performing preliminary affinity characterization or in-depth thermodynamic analysis, this facility enables researchers to quantify binding interactions, protein stability, and molecular structure.
Key Equipment & Capabilities:
- Isothermal Titration Calorimeters (ITC) (x3) – Measures binding enthalpy, entropy, and affinity in protein-protein, protein-ligand, and nucleic acid interactions.
- Surface Plasmon Resonance (OpenSPR) – Provides real-time, label-free binding affinity measurements, critical for kinetic and affinity characterization of biomolecular interactions.
- Multi-Angle & Dynamic Light Scattering (MALS/DLS) – Determines molecular size, aggregation state, and conformational stability of proteins and macromolecular complexes.
- Analytical Ultracentrifuges – Used for molecular weight determination and hydrodynamic analysis of proteins in solution.
- Circular Dichroism (CD) Spectrometer – Analyzes protein secondary structure and folding properties, essential for structural biology and stability studies.
- Biocomp Gradient Station – Supports protein purification, crosslinking experiments, and density gradient fractionation for biomolecular characterization.
- Fluorometers – Quantifies binding affinities and protein stability, providing fluorescence-based assessments of biomolecular interactions.
This facility is crucial for structural biology, drug discovery, and biophysical studies, enabling researchers to characterize macromolecular interactions with high precision.
For McGill lab users, unsupervised access is available at $10/hour. Prior training and booking are required for equipment usage.