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

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 SE I) and non-selective (R 1 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 1 SE and R 1 NS analysis allowed the definition of the affinity index, [A] L T , an index related to the extent of the macromolecule-ligand recognition process.