期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 38, 期 -, 页码 888-893出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST0380888
关键词
biomolecular interaction; drug design; enthalpic efficiency; isothermal titration calorimetry (ITC); lead optimization
资金
- G. Harold and Leila Y. Mathers Foundation
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 naive. 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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