We present analysis of nanosecond-picosecond dynamics of Green Fluorescence Protein (GFP) using neutron scattering data obtained on three spectrometers. GFP has a beta-barrel structure that differs significantly from the structure of other globular proteins and is thought to result in a more rigid local environment. Despite this difference, our analysis reveals that the dynamics of GFP are similar to dynamics of other globular proteins such as lysozyme and myoglobin. We suggest that the same general concept of protein dynamics may be applicable to all these proteins. The dynamics of dry protein are dominated by methyl group rotations, while hydration facilitates localized diffusion-like motions in the protein. The latter has an extremely broad relaxation spectrum. The nanosecond-picosecond dynamics of both dry and hydrated GFP are localized to distances of similar to 1-3.5 angstrom, in contrast to the longer range diffusion of hydration water.