DYNAMICS OF A GLOBULAR PROTEIN AS STUDIED BY NEUTRON-SCATTERING AND SOLID-STATE NMR

Effect of hydration on the dynamics of pan-albumin, a 11.5 kDa Ca2+/Mg 2+-binding globular protein has been studied, at room temperature, by incoherent quasi-elastic neutron scattering and C-13 solid-state NMR. Samples were protein powders hydrated at different hydration levels, T he increase of the quasi-elastic signal observed in neutron scattering upon hydration is interpreted as art increase of the local mobility o f charged side-chain protons (Asp, Glu, Lys) and is in agreement with a parallel study of parvalbumin by solid-state natural abundance C-13 NMR under cross-polarization and magic angle spinning (CP MAS) conditi ons.