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_1~(SE)) and non-selective (R_1~(NE)) 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~(NE) analysis allowed the definition of the "affinity index", [A]_L~T , an index related to the extent of the macromolecule-ligand recognition process.