Comparative study of protein dynamics in hydrated powders and in solutions: A neutron scattering investigation

Abstract Neutron scattering spectroscopy on a time-of-flight spectrometer has been exploited to reveal the vibrational and relaxational spectral contributions of lysozyme in hydrated powder and solution states. The inelastic component of the dynamical structure factor seems to be quite similar for lysozyme in both the solid- and the liquid-state samples, particularly for energies higher than ∼4 meV. After the subtraction of this component, the quasielastic contribution is evaluated. In the case of hydrated lysozyme powder the quasielastic scattering follows a two-power law with a ballistic Gaussian decrease above ∼2 meV. The quasielastic scattering of lysozyme in solution exhibits a rather similar trend but a much larger intensity. This may be related to the increase of both the number and the amplitudes of the confined diffusive processes related to protein side-chains motions at the protein surface.