We used IN16 to study ps-ns dynamics in lyophilized proteins (apoferritin, green fluorescent protein, superoxide dismutase and insulin) and the effect of secondary structure on CH3 activation By operating IN16 in elastic fixed window, EFW, and inelastic fixed window, IFW, modes we showed that while only CH3 activation is apparent in Apo, a more enhanced, possibly structure dependent, dynamic environment is evident in Ins, SOD and GfP. The origin of this extra component is unclear. Our results are in line with NMR studies of non-CH3 side groups However, they are inconsistent with work published from other lyophilized proteins (e.g. lysosyme) This discrepancy may be due to the fact that, unlike previous works, no H/D exchange of unbound labile protons was performed during dialysis of our samples If correct, labile protons contribute considerably to a dynamic landscape in lyophilized material To test this hypothesis, we now ask for time on IN16b to perform complementary EFW / IFW measurements on the proteins mentioned above but dialyzed against D20 to removed scattering intensity from labile species (NH2, OH etc)