title: Computational study of ligand binding to protein receptors.
abstract: We have determined, for the first time, the enthalpic contributions to the energy change associated with ligand reorganization (LR) upon the binding of the same ligand to multiple sites within human serum albumine (HSA). Quantum mechanics based density functional theory (DFT) has been used for the LR calculations, which provides much better accuracy than previously used molecular mechanics methods (MM). Our findings show that for some ligands these enthalpic contributions can be attributed to specific structural and conformational changes.
authors.affiliation: Faculty of Science, Charles Sturt University, Leeds Pde, Orange, NSW 2800, Australia.
authors.forename: Paul
authors.initials: P
authors.lastname: Wembridge
authors.forename: Heather
authors.initials: H
authors.lastname: Robinson
authors.forename: Igor
authors.initials: I
authors.lastname: Novak
mesh_terms: D019342:Acetic Acid / Q000737:chemistry; D000838:Anions; D020134:Catalytic Domain; D019295:Computational Biology / Q000379:methods; D003198:Computer Simulation; D006358:Hot Temperature; D008024:Ligands; D008956:Models, Chemical; D008968:Molecular Conformation; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D011789:Quantum Theory; D015203:Reproducibility of Results; D013816:Thermodynamics
chemical_list: D000838:Anions; D008024:Ligands; D011506:Proteins; D019342:Acetic Acid