Protein Interactions Analysis
The Protein Interactions Analysis capability enables the study of protein-protein and protein-ligand interactions using various techniques including, analytical ultracentrifugation, to determine the native mass, stoichiometry and shape of proteins and biomolecular complexes in solution, isothermal titration microcalorimetry (ITC) and microscale thermophoresis (MST) to measure the thermodynamics of the interactions, and surface plasmon resonance (SPR) spectroscopy to measure binding kinetics.
Instrumentation
Applications
There are a broad range of research questions that can be addressed within this capability:
- Circular Dichroism:
- 2° structure: α, β, turn & random
- Determine if protein/peptide is folded
- Thermal denaturation
- Isothermal Titration Microcalorimetry:
- Thermodynamic parameters: ΔG, KD, ΔH, ΔS & N
- Analytical Ultracentrifugation:
- sedimentation coefficient (s)
- diffusion coefficient (D)
- mass (M)/oligomeric state
- shape (f/f0)
- rate constants (kon/koff)
- native mass (M) (accurate)
- oligomeric state
- affinity of interactions (KD)
- stoichiometry (N)
- sample stability
- Microscale Thermophoresis:
- Affinity (KD)
- Stoichiometry (N)
- Enzyme Kinetics (KM, Kcat)
- ΔG, ΔH & ΔS (van’t Hoff method)
- surface plasmon resonance:
- Rate constants (kon, koff)
- Affinity (KD)
Access
Contact us to discuss your research applications:
- Research Contracts for bespoke projects
- Academic collaboration
Contact Us
For more information and to discuss your requirements please contact:
Dr Jason Paxman
- T: +61 3 9479 2574
- E: J.Paxman@latrobe.edu.au
- W: https://scholars.latrobe.edu.au/jpaxman
Professor Marc Kvansakul
- T: +61 3 9479 2263
- E: M.Kvansakul@latrobe.edu.au
- W: https://scholars.latrobe.edu.au/mkvansakul