Abstract
We present quasi-elastic incoherent neutron scattering data on wet lysozyme powders at water contents (grams of water/grams of protein) of h = 0.20 and 0.45, corresponding to hydration levels below and above the full monolayer coverage of the protein surface. The data were collected under H 2O and D 2O hydration condition; using the IRIS spectrometer with a resolution of 11 μeV (full-width). From spectra for the D 2O hydrated sample we obtain information on the protein dynamics. These spectra are used to separate from the H 2O hydrated sample the contribution due to the hydration water. We show that at low hydration the dynamics of water is very slow and on the same time scale as that of the protein dynamics, while at higher hydration the water molecules show a faster dynamics. The results support the idea that there are clusters of hydration water.
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