Simple sugars are remarkably effective at preserving protein and enzymatic structures against thermal and hydrostatic stress. Here, we investigate the hydrodynamic and biopreservative properties of three small cyclic molecules: glucose, myo-inositol, and methyl-alpha-D-glucopyranoside using circular dichroism spectroscopy and isothermal calorimetry. Using ultrafast fluorescence frequency upconversion spectroscopy, we measure the dynamical retardation of hydration dynamics in cosolute solutions. We find that all three molecules are effective modifiers of hydration dynamics in solution and all are also effective at protecting model protein systems against thermal denaturation. Methyl-alpha-D-glucopyranoside is found to be the most effective dynamic reducer displaying an approximately 30% increase in solvation relaxation time as compared to water in a cosolute free solution. myo-Inositol and glucose both exhibit a smaller reduction in dynamics with similar magnitudes of concentration dependence. Using these cosolute models, we demonstrate that the thermal enhancement of protein structure does not correlate strongly with either the dynamical reduction of the bulk solution nor with the number of hydrogen bonds a cosolute makes with the solvent. Furthermore, solutions of glucose at twice the concentration of trehalose are shown to have similar magnitudes of dynamical impact. This implies that regulation of hydration dynamics is not a distinguishing characteristic of successful osmolytes. This work highlights the need for further studies and computational analysis to understand the phenomena of preferential exclusion and the contribution of hydration dynamics to protein structural stability.