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Mossbauer spectroscopy and neutron scattering measurements on proteinsembedded in solvents including water and aqueous mixtures have emphasized theobservation of the distinctive temperature dependence of the atomic mean squaredisplacements, <u2>, commonly referred to as the dynamic transition at sometemperature Td. At low temperatures, <u2> increases slowly, but it assumestronger temperature dependence after crossing Td, which depends on thetime/frequency resolution of the spectrometer. Various authors have madeconnection of the dynamics of solvated proteins including the dynamictransition to that of glass-forming substances. Notwithstanding, no connectionis made to the similar change of temperature dependence of <u2> obtained byquasielastic neutron scattering when crossing the glass transition temperatureTg, generally observed in inorganic, organic and polymeric glass-formers.Evidences are presented to show that such change of the temperature dependenceof <u2> from neutron scattering at Tg is present in hydrated or solvatedproteins, as well as in the solvents used unsurprisingly since the latter isjust another organic glass-formers. The <u2> obtained by neutron scattering atnot so low temperatures has contributions from the dissipation of moleculeswhile caged by the anharmonic intermolecular potential at times beforedissolution of cages by the onset of the Johari-Goldstein beta-relaxation. Theuniversal change of <u2> at Tg of glass-formers had been rationalized bysensitivity to change in volume and entropy of the beta-relaxation, which ispassed onto the dissipation of the caged molecules and its contribution to<u2>. The same rationalization applies to hydrated and solvated proteins forthe observed change of <u2> at Tg.

Evidence of coexistence of change of caged dynamics at Tg and the dynamic transition at Td in solvated proteins