Quasielastic neutron scattering study on low-hydrated myoglobin inside silica nanopores

In this study, nanosecond-scale dynamics of low-hydrated myoglobin (Mb) encapsulated in mesoporous silica (MPS) with 7.8 nm pores was investigated by using high resolution (energy resolution: 1 μeV) neutron backscattering spectroscopy. The apparent hydration level of the encapsulated myoglobin was 0.06, which was deduced by assuming a uniform distribution of water within myoglobin encapsulated mesoporous silica. The mean square displacement of myoglobin derived from an elastic fixed-window scan was essentially proportional to temperature in the range 120–300 K, indicating the absence of dynamical transition induced by the onset of translational diffusion in the hydration D2O. Since the width of quasielastic neutron scattering (QENS) peaks of the encapsulated Mb was Q-independent at 220, 240, and 265 K, the observed nanosecond-scale dynamics was attributed to internal motions of the encapsulated Mb, such as slow motions of amino acid groups or side chains. The fraction of immobile H-atoms in Mb was estimated to be above 0.8, which was larger than that for a free protein with a similar molecular weight to Mb. The large immobile fraction indicates that the nanosecond-scale motions of amino acid residues and side chains in the vicinity of the pore wall are restricted by the interfacial interactions with the rigid pore wall.