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With continuously improving signal-to-noise ratios, a statistically sound analysis of quasi-elasticneutron scattering (QENS) spectra requires to fit increasingly complex models which poses several challenges.Simultaneous fits of the spectra for all recorded values of the momentum transfer become a standard approach.Spectrometers at spallation sources can have a complicated non-Gaussian resolution function which has to bedescribed most accurately. At the same time, to speed up the fitting, an analytical convolution with this resolutionfunction is of interest. Here, we discuss basic concepts to efficient approaches for fits of QENS spectra basedon standard MATLAB and Python fit algorithms. We illustrate the fits with example data from IN16B, BASIS,and BATS.

The formation of molecular assemblies in protein solutions is of strong interest both from a fundamental viewpoint and for biomedical applications. While ordered and desired protein assemblies are indispensable for some biological functions, undesired protein condensation can induce serious diseases. As a common cofactor, the presence of salt ions is essential for some biological processes involving proteins, and in aqueous suspensions of proteins can also give rise to complex phase diagrams including homogeneous solutions, large aggregates, and dissolution regimes. Here, we systematically study the cluster formation approaching the phase separation in aqueous solutions of the globular protein BSA as a function of temperature (T), the protein concentration (c(p)) and the concentrations of the trivalent salts YCl3 and LaCl3 (c(s)). As an important complement to structural, i.e. time-averaged, techniques we employ a dynamical technique that can detect clusters even when they are transient on the order of a few nanoseconds. By employing incoherent neutron spectroscopy, we unambiguously determine the short-time self-diffusion of the protein clusters depending on c(p), c(s) and T. We determine the cluster size in terms of effective hydrodynamic radii as manifested by the cluster center-of-mass diffusion coefficients D. For both salts, we find a simple functional form D(c(p), c(s), T) in the parameter range explored. The calculated inter-particle attraction strength, determined from the microscopic and short-time diffusive properties of the samples, increases with salt concentration and temperature in the regime investigated and can be linked to the macroscopic behavior of the samples.

Perovskite-type oxyhydrides, BaTiO3-xHx, represent a novel class of hydride ion conducting materials of interest for several electrochemical applications, but fundamental questions surrounding the defect chemistry and hydride ion transport mechanism remain unclear. Here we report results from powder X-ray diffraction, thermal gravimetric analysis, nuclear magnetic resonance spectroscopy, inelastic neutron scattering (INS), and density functional theory (DFT) simulations on three metal hydride reduced BaTiO3 samples characterized by the simultaneous presence of hydride ions and oxygen vacancies. The INS spectra are characterized by two predominating bands at around 114 (omega(perpendicular to)) and 128 (omega(parallel to)) meV, assigned as fundamental Ti-H vibrational modes perpendicular and parallel to the Ti-H-Ti bond direction, respectively, and four additional, weaker, bands at around 99 (omega(1)), 110 (omega(2)), 137 (omega(3)) and 145 (omega(4)) meV that originate from a range of different local structures associated with different configurations of the hydride ions and oxygen vacancies in the materials. Crucially, the combined analyses of INS and DFT data confirm the presence of both nearest and next-nearest neighbouring oxygen vacancies to the hydride ions. This supports previous findings from quasielastic neutron scattering experiments, that the hydride ion transport is governed by jump diffusion dynamics between neighbouring and next-nearest neighbouring hydride ion-oxygen vacancy local structures. Furthermore, the investigation of the momentum transfer dependence of the INS spectrum is used to derive the mean square displacement of the hydride ions, which is shown to be in excellent agreement with the calculations. Analysis of the mean square displacement confirms that the hydrogen vibrational motions are localized in nature and only very weakly affected by the dynamics of the surrounding perovskite structure. This insight motivates efforts to identify al

Molecular dynamics plays an important role for the biological function of proteins. For protein ligand interactions, changes of conformational entropy of protein and hydration layer are relevant for the binding process. Quasielastic neutron scattering (QENS) was used to investigate differences in protein dynamics and conformational entropy of ligand-bound and ligand-free streptavidin. Protein dynamics were probed both on the fast picosecond time scale using neutron time-of-flight spectroscopy and on the slower nanosecond time scale using high-resolution neutron backscattering spectroscopy. We found the internal equilibrium motions of streptavidin and the corresponding mean square displacements (MSDs) to be greatly reduced upon biotin binding. On the basis of the observed MSDs, we calculated the difference of conformational entropy Delta S-conf of the protein component between ligand-bound and ligand-free streptavidin. The rather large negative Delta S-conf value (-2 kJ mol(-1) K-1 on the nanosecond time scale) obtained for the streptavidin tetramer seems to be counterintuitive, given the exceptionally high affinity of streptavidin-biotin binding. Literature data on the total entropy change Delta S observed upon biotin binding to streptavidin, which includes contributions from both the protein and the hydration water, suggest partial compensation of the unfavorable Delta S-conf by a large positive entropy gain of the surrounding hydration layer and water molecules that are displaced during ligand binding.

Perovskite-type oxyhydrides, BaTiO3-xHx, have been recently shown to exhibit hydride-ion (H-) conductivity at elevated temperatures, but the underlying mechanism of hydride-ion conduction and how it depends on temperature and oxygen vacancy concentration remains unclear. Here, we investigate, through the use of quasielastic neutron scattering techniques, the nature of the hydride-ion dynamics in three metal hydride-reduced BaTiO3 samples that are characterized by the simultaneous presence of hydride ions and oxygen vacancies. Measurements of elastic fixed window scans upon heating reveal the presence of quasielastic scattering due to hydride-ion dynamics for temperatures above ca. 200 K. Analyses of quasielastic spectra measured at low (225 and 250 K) and high (400-700 K) temperature show that the dynamics can be adequately described by established models of jump diffusion. At low temperature, <= 250 K, all of the models feature a characteristic jump distance of about 2.8 angstrom, thus of the order of the distance between neighboring oxygen atoms or oxygen vacancies of the perovskite lattice and a mean residence time between successive jumps of the order of 0.1 ns. At higher temperatures, >400 K, the jump distance increases to about 4 angstrom, thus of the order of the distance between next-nearest neighboring oxygen atoms or oxygen vacancies, with a mean residence time of the order of picoseconds. A diffusion constant D was computed from the data measured at low and high temperatures, respectively, and takes on values of about 0.4 X 10(-6) cm(-2) s(-1) at the lowest applied temperature of 225 K and between ca. 20 X 10(-6) and 100 X 10(-6) cm(-2) s(-1) at temperatures between 400 and 700 K. Activation energies E-a were derived from the measurements at high temperatures and take on values of about 0.1 eV and show a slight increase with increasing oxygen vacancy concentration.

As a consequence of its ordered pore architecture, mesoporous SBA-15 offers new possibilities for incorporating biological agents. Considering its applicability in oral vaccination, which shows more beneficial features when compared with parenteral vaccines, SBA-15 is also seen as a very promising adjuvant to carry, protect, and deliver entrapped antigens. Recent studies have shown several remarkable features in the immunization of hepatitis B, a viral disease transmitted mainly through blood or serum transfer. However, the surface antigen of the hepatitis B virus, HBsAg, is too large to fit inside the SBA-15 matrix with mean pore diameter around 10 nm, thus raising the question of how SBA-15 can protect the antigen. In this work, thermal analysis combined with neutron spectroscopy allowed us to shed light on the interactions between HBsAg and SBA-15 as well as on the role that these interactions play in the efficiency of this promising oral vaccination method. This information was obtained by verifying how the dynamic behaviour of the antigen is modified under confinement in SBA-15, thus also establishing an experimental method for verifying molecular dynamics simulations.

In this work lithium self-diffusion in the model lithium garnet oxide Li 5 La 3 Ta 2 O 12 was investigated by combining quasi-elastic neutron scattering experiments and molecular dynamics simulation. The Q-dependence of the quasi-elastic broadening measured experimentally and of the mean relaxation rate of lithium calculated by molecular dynamics simulations were both well described by the Singwi-Sjölander diffusion model. This model describes lithium nuclei that undergo diffusion via a jump-type mechanism consisting of a distribution of jumps with a mean square jump distance and residence time. The extracted mean jump length is consistent with a jump between tetrahedral (24d) to octahedral (48g and 96h) sites within the Ia3¯d symmetry structure and the residence time of Li at these sites obeys an Arrhenius relation from ~ ps timescales at 1100 K to the ~ ns range at 400 K. This result supports a lithium diffusion mechanism in which jumps are more frequent (smaller residence time) and shorter at higher temperature. The self-diffusivities of Li from both experiment and calculation were in good agreement, but deviations from those previously measured using nuclear magnetic resonance and muon spin relaxation were observed and discussed. Analysis of stretching parameter describing the relaxation of lithium calculated by molecular dynamics indicated that Li motion is more cooperative at shorter length scales, below ~ 4.4 Å, which corresponds to the distance between octahedral sites across the tetrahedral site.