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While the measurement of thermodynamic properties has become routine, the information they provide is often complex and not fully understood. Join Dr. Ladbury to explore how thermodynamic data can enhance our understanding of protein-ligand interactions.
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Isothermal Titration Calorimetry is the most sensitive method for characterizing binding interactions. Reveal how ITC precisely analyzes molecular interactions, which provides crucial thermodynamic data to understand physiological processes and develop new strategies.
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Pharmaceutical research and discovery rely on accurate characterization of molecular interactions. Discover an Isothermal Titration Calorimetry tool that is precise for characterizing, which is crucial for drug discovery and lead optimization in research.
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All biochemical reactions involve recognition, binding, and the formation of non-covalent complexes. Uncover a powerful technique for analyzing biochemical binding events that is crucial for understanding molecular interactions and enzyme kinetics in biomedical research.
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Enthalpy screen, incremental titration, and continuous titration were utilized on the Affinity ITC to characterize the binding of Furosemide and Carbonic Anhydrase II. Examine the experiment results to see how these three ITC methods compare.
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