Differential line-broadening and T₂ relaxation data ( 97EMBO1436, 99JACS9903, and 00JMB1023-295). Binding of a small molecule to a large protein will cause the ligand T₂ values to decrease and the signals to broaden. The degree of broadening observed is dependent on the affinity of the ligand for the protein.

Determination of the bound ligand conformation using transferred cross-correlated relaxation ( 05ARB245).

A transferred 13C T1 relaxation study has been applied for determining the changes of relaxation rates upon binding to a macromolecule ( 00JACS12530).

A NMR method based on the combination of transverse and/or selective longitudinal relaxation parameters and competition binding experiments has been proposed for screenin purposes ( 02JACS7702).

A revision work with dynamic changes upon binding in protein-metal ion, -small molecules, -peptides, and -nucleic acid complexes has been appeared ( 01ACR379)

The introduction of an spin-label target strongly alter the relaxation properties of its surrounding

Other applications:

• Anisotropic rotational diffusion for a ternary DHFR complex ( 01JB209)
• Affinity index determination from relaxation data ( 01MRC457)
• NMRKIN. A program to simulate line shapes from 2D spectra of proteins upon ligand binding ( 02JB201-22)
• Selective and non-selective T1 measurements to monitor the affinity of ligand-receptor complexes ( 01MRC457)