Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7901788 | Journal of Non-Crystalline Solids | 2015 | 7 Pages |
Abstract
The vibrational dynamics of protein hydration water has been studied by incoherent neutron scattering. Experiments on a sample of fully deuterated maltose binding protein allowed us to single out the hydration water susceptibility. The main inelastic features, corresponding to hydrogen-bond bending, hydrogen-bond stretching and librational excitations, have been followed over a temperature range extending from 50 to 300Â K. It turns out that the temperature dependence of the hydrogen-bond stretching contribution is quite similar to that of the mean square displacements deduced by the quasielastic signal, thus suggesting a close relationship between the anharmonicity of longitudinal phonon-like motions and the onset of diffusive molecular dynamics. On the other hand, both hydrogen-bond bending and librational excitations show a temperature dependence consistent with a harmonic character over the whole temperature range.
Keywords
Related Topics
Physical Sciences and Engineering
Materials Science
Ceramics and Composites
Authors
Alessandro Paciaroni, Andrea Orecchini, Federico Sebastiani, Simone Capaccioli, Kia L. Ngai, Martine Moulin, Michael Haertlein, Caterina Petrillo, Francesco Sacchetti,