Water plays a critical role in determining the structure and function of biological system. A hydration level, h~0.2 g water/g protein, is often found to be the minimum requirement for the dynamical transition in protein at ~200K. However, we have demonstrated that dry proteins also present a dynamical transition around 200 K if measured in the perdeuterated state by neutron scattering. This transition is absent in the dry hydrogenated protein due to the strong contribution of methyl rotations. Our results suggest that, as long as one can remove the contribution from methyl motions, the dynamical transition will be evident in the dry state. Using a neutron instrument with a low energy resolution such that methyl rotations cannot be resolved, e.g., ~100ueV, such as OSIRIS with PG004 reflection will assist us in analyzing the origin and influence of this dynamical transition in dry state.