ABSTRACT

This chapter attempts to deal primarily with the study of ligand-protein interactions by nuclear magnetic resonance (NMR) techniques. The magnetic resonance phenomena contain three principle parameters that reflect useful information; the chemical shift, coupling constants, and relaxation rates. The judicious applications of nuclear relaxation rates can result in kinetic, thermodynamic, and structural information concerning the formation of enzyme-ligand complexes. A description of the NMR phenomena can be provided via a quantum mechanical approach or a classical mechanical description. The utilization of nuclear relaxation techniques using a paramagnetic probe can be used to study specific ligand-protein interactions. Studies can be performed by indirect measurements-observing the paramagnetic effect on the solvent, or by direct measurements of the ligand itself. The characterization of an enzyme-metal complex can be performed, under ideal circumstances, to obtain a wealth of information concerning this binary complex.