ABSTRACT
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Relaxation measurements have found a widespread use in many different areas within the fields of physics, chemistry, and biology. There are not many methods by which dynamics on the time scale afforded by nuclear spin relaxation can be studied; many of the advances within the field of relaxation have therefore been focused on reliable determination of molecular dynamic parameters. In the field of biomolecular NMR, the possibility to produce isotope-labeled compounds has opened up for extensive studies of local dynamics in biological systems. The development of models for interpreting relaxation data in terms of dynamic parameters has made these investigations particularly useful for investigating protein backbone dynamics.
