Changes in relaxation data is an usual way to study binding properties of macromolecular complexes. A revision work with dynamic changes upon binding in protein-metal ion, -small molecules, -peptides, and -nucleic acid complexes has been appeared ( 01ACR379).

Protein dynamics in supercooled water ( 02JB63-23)

Calculation of hydrodynamic properties of proteins using bead models (HYDRONMR) ( 00JMR138-147 ). Interpretation of 15N relaxation data of globular proteins ( 02JB139-23 ).

Thermodynamic interpretation of NMR relaxation data ( 00JPCB11416 )

Differential multiple-quantum relaxation caused by chemical exchange ( 02JB263-24 )

NMR relaxation dispersion studies in biomolecular solutions ( 01METH178-338 )