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.
	Screening of lead candidates in drug discovery.
	Evaluation of the association and dissociation rates and the half-life complex measurements.
	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.

Surname	Name	Location	Phone number	Email
TAULÉS MARIN (*)	MARTA	Edifici Clúster (PCB) C/ Baldiri Reixac, 10	934037200	marta@ccit.ub.edu

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