Dynamics of proteins
NMR is the method of choice to study protein dynamics on a time scale of 15 orders of magnitude by various relaxation methods. Protein functions is directly related to the internal dynamics of proteins, which we could show for the cold shock protein CspB, the metallochaperone SlyD, and the human CDK inhibitor p19INKd. Intermolecular interactions between proteins e.g. at high concentrations of under molecular crowding conditions could be revealed for eye lens crystallins by studies of the translational and rotational dynamics.
NMR time scale and corresponding dynamics of proteins.