Molecular interaction analysis
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Surface Plasmon Resonance (SPR), real time and label-free interaction analysis.
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Set up for every pair of molecules: optimization of the ligand immobilization (way and density to be immobilized), reference channel, buffer running and temperature.
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Optimization of strategies to obtain the best results in accordance the source of the samples: qualitative or quantitative perspectives.
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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.
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Screening of lead candidates in drug discovery.
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Evaluation of the association and dissociation rates and the half-life complex measurements.
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Thermodynamic analysis.
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Determination of the binding domain for the analysis of different mutants against targets.
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Effect of cofactors, metal ions and other molecules against the binding kinetics.
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Toxin detection.
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Characterization of immune response.
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Effect (in kinetics terms) of different modifications of antibodies.
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Surname
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Name
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Location
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Phone number
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Email
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TAULÉS MARIN (*)
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MARTA
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Edifici Clúster (PCB) C/ Baldiri Reixac, 10
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934037200
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marta@ccit.ub.edu
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(*) For more information
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