By combining OSIRIS/IN16 elastic window and QENS data we better understand dynamics in lyophilised apoferritin. This complimentary approach reveals that the observed decrease in elastic scattering intensity, I(Q, 100<T<300K), is due to CH3 dynamics. To compliment this work we wish to study the interplay of structure and protein dynamics. We have used OSIRIS to probe an-harmonic behaviour in superoxide dismutase (SOD, helical secondary structure) and green fluorescent protein (GFP, non-helical beta-sheet). Unlike apoferritin, both proteins show a decrease in I(Q,100<T<300K) which cannot be described simply using a CH3-activation model. This result suggests the presence of additional dynamic contributions. The OSIRIS energy resolution is insufficient to separate additional dynamic components. We therefore seek access to higher energy resolution spectroscopy (IRIS) to elucidate a difference