title: Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design.
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.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Texas MD Anderson Cancer Center, Unit 1000, 1515 Holcombe Boulevard, Houston, TX 77030, USA. jeladbury@mdanderson.org
authors.forename: John E
authors.initials: JE
authors.lastname: Ladbury
mesh_terms: D000818:Animals; D002151:Calorimetry / Q000379:methods* / Q000706:statistics & numerical data*; D032882:Comprehension; D015195:Drug Design; D004347:Drug Interactions; D006801:Humans; D008024:Ligands; D046911:Macromolecular Substances / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods; D013816:Thermodynamics
chemical_list: D008024:Ligands; D046911:Macromolecular Substances