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A low-temperature dynamical transition has been reported in several proteins.We provide the first observation of a `protein-like' dynamical transition innonbiological aqueous environments. To this aim we exploit the popularcolloidal system of poly-N-isopropylacrylamide (PNIPAM) microgels, extendingtheir investigation to unprecedentedly high concentrations. Owing to theheterogeneous architecture of the microgels, water crystallization is avoidedin concentrated samples, allowing us to monitor atomic dynamics at lowtemperatures. By elastic incoherent neutron scattering and molecular dynamicssimulations, we find that a dynamical transition occurs at a temperature$T_d\sim250$~K, independently from PNIPAM mass fraction. However, thetransition is smeared out on approaching dry conditions. The quantitativeagreement between experiments and simulations provides evidence that thetransition occurs simultaneously for PNIPAM and water dynamics. The similarityof these results with hydrated protein powders suggests that the dynamicaltransition is a generic feature in complex macromolecular systems,independently from their biological function.

Evidence of a low-temperature dynamical transition in concentrated microgels