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We present a pressure dependence study of the dynamics of lysozyme proteinpowder immersed in deuterated $\alpha$,$\alpha$-trehalose environment viaquasi-elastic neutron scattering (QENS). The goal is to assess thebaro-protective benefits of trehalose on bio-molecules by comparing thefindings with those of a trehalose-free reference study. While the mean-squaredisplacement of the trehalose-free protein (hydrated to $d_{D_2O}\simeq$40 w\%)as a whole, is reduced by increasing pressure, the actual observable relaxationdynamics in the pico-(ps) to nano-seconds (ns) time range remains largelyunaffected by pressure - up to the maximum investigated pressure of 2.78(2)Kbar. Our observation is independent of whether or not the protein is mixedwith the deuterated sugar. This suggests that the hydrated protein'sconformational states at atmospheric pressure remain unaltered by hydrostaticpressures, below 2.78 Kbar. We also found the QENS response to be totallyrecoverable after ambient pressure conditions are restored. Circular dichroismand neutron diffraction measurements confirm that the protein structuralintegrity is conserved and remains intact, after pressure is released. Weobserve however a clear narrowing of the quasi-elastic neutron (QENS) responseas the temperature is decreased from 290 K to 230 K in both cases, which weparametrize using the Kohlrausch-Williams-Watts (KWW) stretched exponentialmodel. Only the fraction of protons that are immobile on the accessible timewindow of the instrument, referred to as the elastic incoherent structurefactor or (EISF) is observably sensitive to pressure, increasing onlymarginally but systematically with increasing pressure.

High pressure dynamics of hydrated protein in bio-protective trehalose environment