Water-protein and ligand-protein interactions as determined by selective NMR relaxation studies

摘要

Water-macromolecules and ligand-macromolecules interactions were investigated considering the effects induced by the presence of a macromolecule on both the water and the ligand NMR selective (R-l(SE)) and non-selective (R-l(NS)) spin-lattice relaxation rates. The results obtained from the solvent studies were used to describe the solvent dynamics at the macromolecule-solvent interface. On the other hand, ligand R-l(SE) and R-l(NS) analysis allowed the definition of the "affinity index", [A](L)(T), an index related to the extent of the macromolecule-ligand recognition process. [References: 22]