Effect of hydration on the dynamics of parvalbumin, a 11.5 kDa Ca2+/Mg2+-binding globular protein has been studied, at room temperature, by incoherent quasi-elastic neutron scattering and 13C solid-state NMR. Samples were protein powders hydrated at different hydration levels. The increase of the quasi-elastic signal observed in neutron scattering upon hydration is interpreted as an increase of the local mobility of charged side-chain protons (Asp, Glu, Lys) and is in agreement with a parallel study of parvalbumin by solid-state natural abundance 13C NMR under cross-polarization and magic angle spinning (CP MAS) conditions.