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.