Time-resolved fluorescence depolarization on the nanosecond and sub-nanosecond time scales is a powerful technique for the study of rapid motions in the condensed phase. We apply this technique to measure the motions of proteins using both extrinsic and intrinsic probes. Eosin, which absorbs and fluoresces in the visible, forms a one-to-one complex with lysozyme binding in the hydrophobic box region and is used as an extrinsic probe of lysozyme motion. The long-time anisotropy of bound eosin is used to measure the overall rotation time of lysozyme for which refined values are presented. In addition, our measurements show a rapid restricted motion of the eosin molecule on the time scale of approximately 100 ps. The order parameter, a model independent measure of the extent of the restriction of the rapid motions, decreases with increasing temperature, indicating that the motion of the eosin is less hindered as temperature increases. We compare our results with the crystallographic measurements of least square displacements for the hydrophobic box region. Our measurements provide direct time resolved confirmation that the displacements observed in this region correspond to rapid motion.