The Thermodynamics of Protein–Ligand Interaction and Solvation: Insights for Ligand Design

• Published in: Journal of molecular biology Vol. 384; no. 4; pp. 1002 - 1017
• Main Authors: Olsson, Tjelvar S.G., Williams, Mark A., Pitt, William R., Ladbury, John E.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 26.12.2008
• Subjects: isothermal titration calorimetry; Ligands; Protein Binding; protein structure; Protein Structure, Quaternary; Proteins - metabolism; protein–ligand interaction; solvent-accessible surface; Thermodynamics; CSA; protein structure; isothermal titration calorimetry; solvent-accessible surface; protein–ligand interaction; thermodynamics; ITC; SCORPIO; SMILES; ASA; PDB

Isothermal titration calorimetry is able to provide accurate information on the thermodynamic contributions of enthalpy and entropy changes to free energies of binding. The Structure/Calorimetry of Reported Protein Interactions Online database of published isothermal titration calorimetry studies an...