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  • Title: Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design.
    Author: Ladbury JE.
    Journal: Biochem Soc Trans; 2010 Aug; 38(4):888-93. PubMed ID: 20658972.
    Abstract:
    The binding of two biomolecules viewed from the atomic level is highly complex. It involves the formation or removal of many individual non-covalent bonds both between the interacting molecules as well as with solvent. Currently, our understanding of the thermodynamic quantification of biomolecular interactions is somewhat naïve. ITC (isothermal titration calorimetry) provides a rapid route to a full thermodynamic characterization of a biomolecular interaction. Armed with these data, what are we really able to understand about complex formation and can any of this information provide a useful tool to aid drug development? Correlations between thermodynamic data and structural detail have been investigated, allowing insight into ways in which these can be used to understand protein-ligand interactions and provide input into the decision-making process in drug development.
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