To probe the details of small amplitude motions in proteins, a dynamic analysis of the orientation fluctuations of 2 tyrosine side chains in the bovine pancreatic trypsin inhibitor is presented. Detailed results are given for the time history and correlation functions obtained for the ring motion from a molecular dynamics simulation of the entire protein. Even on a picosecond time scale orientational fluctuations of .+-. 30.degree. from the average position occur for the tyrosine rings in the interior of the protein. The Langevin equation is applicable to the ring torsional motion, which corresponds to that of an angular harmonic oscillator with near-critical damping. Two possible microscopic models for the observed damping effects are outlined. One of these, analogous to liquid behavior, is based on kinetic theory and takes account of the collisions which occur between atoms of the protein; the other, more analogous to solid behavior, involves the coupling among a large number of harmonic oscillators. The collisional model with parameters obtained from theoretical estimates leads to good agreement with the correlation functions from the dynamic simulation. However, the dephasing of harmonic oscillations can yield similar short-time results so that a distinction between the 2 models is difficult. The importance of damping effects on the motions involved in conformational transitions and enzymatic reactions is discussed.