Molecular interaction analysis
- Surface Plasmon Resonance (SPR), real time and label-free interaction analysis.
- Set up for every pair of molecules: optimization of the ligand immobilization (way and density to be immobilized), reference channel, buffer running and temperature.
- Optimization of strategies to obtain the best results in accordance the source of the samples: qualitative or quantitative perspectives.
- Evaluation of the rates constants (kon, koff) and equilibrium constants (KA, KD) in different models: protein/DNA, protein/protein, protein/peptide, carbohydrate/protein, RNA/DNA.
- Selection of active ingredients in pharmacological research.
- Thermodynamic analysis.
- Determination of the binding domain for the analysis of different mutants against targets.
- Effect of cofactors, metal ions and other molecules against the binding kinetics.
- Toxin detection.
- Characterization of immune response.
- Effect (in kinetics terms) of different modifications of antibodies.
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