Sample interview questions: Can you discuss any experience you have in studying the interactions between biomolecules using techniques like surface plasmon resonance or isothermal titration calorimetry?
Sample answer:
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Surface Plasmon Resonance (SPR)
- Utilized SPR to investigate the binding kinetics and affinity of protein-protein interactions, including those involving receptors and ligands, antibodies and antigens, and enzymes and substrates.
- Designed and optimized SPR experiments to determine kinetic parameters such as association and dissociation rates, equilibrium dissociation constants (KD), and binding stoichiometry.
- Performed data analysis and interpretation using specialized software to extract quantitative information about the interactions under study.
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Isothermal Titration Calorimetry (ITC)
- Employed ITC to measure the thermodynamic parameters of biomolecular interactions, including binding enthalpy (ΔH), binding entropy (ΔS), and binding free energy (ΔG).
- Conducted ITC experiments under controlled temperature conditions to obtain accurate and reliable thermodynamic data.
- Analyzed ITC data using appropriate software to determine binding stoichiometry, thermodynamic parameters, and the nature of the interactions (e.g., exothermic or endothermic).
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