This review surveys recent investigations of conformational fluctuations of
proteins in solution using NMR techniques. Advances in experimental method
s have provided more accurate means of characterizing fast and slow interna
l motions as well as overall diffusion. The information obtained from NMR d
ynamics experiments provides insights into specific structural changes or c
onfigurational energetics associated with function. A variety of applicatio
ns illustrate that studies of protein dynamics provide insights into protei
n-protein interactions, target recognition, ligand binding, and enzyme func
tion.