title: Site-specific free energy changes in proteins upon ligand binding by nuclear magnetic resonance: Ca2+ -displacement by Ln3+ in a Ca2+ -binding protein from Entamoeba histolytica.
abstract: The study of protein-ligand interaction has been of a great interest in contemporary structural biology. The understanding of the nature of such interaction and determining the associated binding affinities are of utmost importance. Nuclear magnetic resonance has become a powerful tool in deriving information related to such interactions in proteins. Nuclear magnetic resonance data provide the site-specific information even in the case of proteins having multiple-binding sites and populations of respective species. In this communication, we set out to use such information to derive the associated microscopic binding constants.
authors.affiliation: Department of Chemical Sciences, Tata Institute of Fundamental Research, Mumbai, India.
authors.forename: Kousik
authors.initials: K
authors.lastname: Chandra
authors.forename: Sourajit M
authors.initials: SM
authors.lastname: Mustafi
authors.forename: Subramanian
authors.initials: S
authors.lastname: Muthukumar
authors.forename: Kandala V R
authors.initials: KV
authors.lastname: Chary
mesh_terms: D002118:Calcium / Q000737:chemistry*; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D004748:Entamoeba histolytica / Q000378:metabolism*; D028581:Lanthanoid Series Elements / Q000737:chemistry*; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011485:Protein Binding; D013379:Substrate Specificity; D013816:Thermodynamics
chemical_list: D002135:Calcium-Binding Proteins; D028581:Lanthanoid Series Elements; D008024:Ligands; C085577:Ca2+-binding protein-1; D002118:Calcium