Hydrated proteins undergo a change in their dynamical properties in the neighborhood of a temperature. The change of dynamics has been likened to glass transition of glass-forming substances because similar properties were found. However, a complete understanding of the conformation fluctuations of hydrated proteins and their relation to the dynamics of the solvent is still not available, possibly due to the protein molecules being more complex than ordinary glass-formers. For this reason, we turn our attention to the experimental findings of the dynamics of mixtures of water with simpler glass-formers (small molecules and polymers). Two major relaxation processes have been observed in these aqueous mixtures. One is the structural alpha-relaxation of the hydrophilic glass-former hydrogen bonded to the water, which is responsible for glass transition. The other one is the local secondary beta-relaxation of water in the mixture. Remarkably, these two relaxation processes in aqueous mixtures have analogues in hydrated proteins with the same properties. The conformation fluctuations of the protein and the relaxation of the solvent in hydrated proteins behave like the alpha-relaxation of the hydrophilic glass-former hydrogen bonded to the water and the beta-relaxation of water in other aqueous mixtures, respectively. At low temperatures, the Arrhenius activation energy of the relaxation time of the solvent in a hydrated protein is almost the same as that of the beta-relaxation of water in the glassy states of aqueous mixtures. The Arrhenius T-dependence of the solvent relaxation times no longer holds at temperatures that exceed the "glass" transition temperature of the hydrated protein, defined as the temperature at which the conformation relaxation time is very long. This behavior of the solvent in hydrated proteins is similar to that found in the beta-relaxation of water in aqueous mixtures when crossing the glass transition temperature of the mixture (Capaccioli, S.; Ngai, K. L.; Shinyashiki, N. J. Phys. Chem. B 2007, 111, 8197). Furthermore, the same dynamics were found in mixtures of two van der Waals glass-formers, which are even simpler systems than aqueous mixtures because of the absence of hydrogen bonding. The experimental data of these ideal mixtures of van der Waals glass-formers have been given a satisfactory theoretical explanation. Since the properties of hydrated proteins, aqueous mixtures, and the mixtures of van der Waals liquids are similar, we transfer the theoretical understanding gained in the study of the last system sequentially to the two other increasingly more complex systems.