Pressure dependence of protein dynamics investigated using elastic and quasielastic neutron scattering

We present here a study of the dynamics of two monomeric proteins, trypsin and lysozyme, by means of elastic and quasielastic neutron scattering under medium-to-high pressure conditions (1-1200 bar). The internal motions as probed from the average proton dynamics in the 100 ps timescale have a confined diffusive nature. On increasing the pressure up to 1200 bar the confinement volume is almost unaffected, while the fraction of protons involved is slightly decreased.