NMR Titrations allow a good estimation of the affinity, stoichiometry and specificity of binding as well as the kinetics of binding. How the chemical shifts of the protein change during the titration is determined by the kinetics of the interaction.

NMR-based characterization of large protein-ligand interactions using NMR-DOC: Nuclear Magnetic Resonance DOcking of Compounds) ( 02JB165-22).

The PDBbind database: Collection of binding affinities for protein-ligand complexes ( 04JMC2977).

Suite of 2D and 3D Nz-exchange NMR experiments for rapidly assigning backbone 1H and 15N amide resonances of the ligand bound form of a protein in a slow exchange with its free state. ( 04JB155-30).