From the above it is evident that upon heating, BSA or mAb in their respective excipient matrix can undergo conformational changes in structure. The composition of the excipient matrix can dictate the strength of these conformational changes, and the relative number of changes is represented by the steepness of the region 2 gradient of the THz spectra. This is dependant on the excipients used and the concentrations added, which influence whether a stronger scaffold is formed for the protein in the dry state. It can be suggested that a strong scaffold can be linked to systems which exhibit a plateau, and for which the protein is confined within the matrix at high temperatures. In contrast, some protein formulations exhibit an increase in absorption. For these the dynamics of the systems exhibit similar behaviour to that of small organic molecules, for which at higher temperatures the vibrational motions of the molecules increases continuously with no confinement of the protein in matrix taking place.