Tobias Unruh

Interaction of hydrogen with accessible metal sites in the metal–organic frameworks M2(dhtp) (CPO-27-M; M = Ni, Co, Mg)

Hydrogen molecules adsorbed in the nickel, cobalt, and magnesium analogs of the CPO-27 metal-organic framework at low loadings interact significantly more strongly than those adsorbed successively as a consequence of the strong interaction of hydrogen with the coordinatively unsaturated metal cations in the framework.

Molecular Mechanism of Long-Range Diffusion in Phospholipid Membranes Studied by Quasielastic Neutron Scattering

The motion of phospholipids has previously been studied on many time scales due to the significance for living cells and technological applications. The motions on a pico- to nanosecond time scale were determined by quasielastic neutron scattering (QENS) to be much faster than the ones on the microsecond scale covered by fluorescence recovery after photobleaching (FRAP). This was explained by assuming that the molecules rattle fast in a cage of neighbors (observed with QENS) from which they escape once in a while; this escape was then the primary step of the slower diffusion measured by FRAP. However, nanosecond MD simulation studies could not observe any escape events; recent findings even suggested that the long-range motion in phospholipid membranes on short time scales is not diffusive but has flow-like characteristics. To check this novel view, we have repeated the QENS experiments with todays significantly improved instrumentation. By using the advantage of QENS that allows tuning of the observation time in the pico- to nanosecond range, it was possible to study the evolution of motions in this time frame. Localized motions, e.g., of the head and tail groups, appear separated from the long-range motion and do not obfuscate the analysis as they do in a mean squared displacement plot. The results for the long-range motion are indeed compatible with flow patterns, whereas the localized motions can account for the fast motions interpreted as motions in a cage before. Hereby, we give experimental evidence for a completely different mechanism of long-range motion on short time scales in phospholipid membranes.

Temperature Dependence of the Primary Relaxation in 1-Hexyl-3-methylimidazolium bis{(trifluoromethyl)sulfonyl}imide

We present results from complementary characterizations of the primary relaxation rate of a room temperature ionic liquid (RTIL), 1-hexyl-3-methylimidazolium bis{(trifluoromethyl)sulfonyl} imide, [C6mim][Tf2N], over a wide temperature range. This extensive data set is successfully merged with existing literature data for conductivity, viscosity, and NMR diffusion coefficients thus providing, for the case of RTILs, a unique description of the primary process relaxation map over more than 12 decades in relaxation rate and between 185 and 430 K. This unique data set allows a detailed characterization of the VTF parameters for the primary process, that are: B=890 K, T0=155.2 K, leading to a fragility index m=71, corresponding to an intermediate fragility. For the first time neutron spin echo data from a fully deuteriated sample of RTIL at the two main interference peaks, Q=0.76 and 1.4 A(-1) are presented. At high temperature (T>250 K), the collective structural relaxation rate follows the viscosity behavior; however at lower temperatures it deviates from the viscosity behavior, indicating the existence of a faster process.

Study of the dynamics of poly(ethylene oxide) by combining molecular dynamic simulations and neutron scattering experiments.

We performed quasielastic neutron scattering experiments and atomistic molecular dynamics simulations on a poly(ethylene oxide) (PEO) homopolymer system above the melting point. The excellent agreement found between both sets of data, together with a successful comparison with literature diffraction results, validates the condensed-phase optimized molecular potentials for atomistic simulation studies (COMPASS) force field used to produce our dynamic runs and gives support to their further analysis. This provided direct information on magnitudes which are not accessible from experiments such as the radial probability distribution functions of specific atoms at different times and their moments. The results of our simulations on the H-motions and different experiments indicate that in the high-temperature range investigated the dynamics is Rouse-like for Q-values below approximately 0.6 A(-1). We then addressed the single chain dynamic structure factor with the simulations. A mode analysis, not possible directly experimentally, reveals the limits of applicability of the Rouse model to PEO. We discuss the possible origins for the observed deviations.

Dynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study

Casein proteins belong to the class of natively disordered proteins. The existence of disordered biologically active proteins questions the assumption that a well-folded structure is required for function. A hypothesis generally put forward is that the unstructured nature of these proteins results from the functional need of a higher flexibility. This interplay between structure and dynamics was investigated in a series of time-of-flight neutron scattering experiments, performed on casein proteins, as well as on three well-folded proteins with distinct secondary structures, namely, myoglobin (α), lysozyme (α/β) and concanavalin A (β). To illustrate the subtraction of the solvent contribution from the scattering spectra, we used the dynamic susceptibility spectra emphasizing the high frequency part of the spectrum, where the solvent dominates. The quality of the procedure is checked by comparing the corrected spectra to those of the dry and hydrated protein with negligible solvent contamination. Results of spectra analysis reveal differences in motional amplitudes of well-folded proteins, where β-sheet structures appear to be more rigid than a cluster of α-helices. The disordered caseins display the largest conformational displacements. Moreover their global diffusion rates deviate from the expected dependence, suggesting further large-scale conformational motions.

Hydration dependent studies of highly aligned multilayer lipid membranes by neutron scattering

We investigated molecular motions on a picosecond timescale of 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) model membranes as a function of hydration by using elastic and quasielastic neutron scattering. Two different hydrations corresponding to approximately nine and twelve water molecules per lipid were studied, the latter being the fully hydrated state. In our study, we focused on head group motions by using chain deuterated lipids. Information on in-plane and out-of-plane motions could be extracted by using solid supported DMPC multilayers. Our studies confirm and complete former investigations by König et al. [J. Phys. II (France) 2, 1589 (1992)] and Rheinstädter et al. [Phys. Rev. Lett. 101, 248106 (2008)] who described the dynamics of lipid membranes, but did not explore the influence of hydration on the head group dynamics as presented here. From the elastic data, a clear shift of the main phase transition from the P(β) ripple phase to the L(α) liquid phase was observed. Decreasing water content moves the transition temperature to higher temperatures. The quasielastic data permit a closer investigation of the different types of head group motion of the two samples. Two different models are needed to fit the elastic incoherent structure factor and corresponding radii were calculated. The presented data show the strong influence hydration has on the head group mobility of DMPC.

Neutron scattering study of the dynamics of a polymer melt under nanoscopic confinement

Poly(ethylene oxide) confined in an anodic aluminum oxide solid matrix has been studied by different neutron scattering techniques in the momentum transfer (Q) range 0.2<or=Q=/Q/<or=1.9 A(-1). The cylindrical pores of the matrix present a diameter (40 nm) much smaller than their length (150 microm) and are parallel and hexagonally ordered. In particular, we investigated the neutron intensity scattered for two orientations of the sample with respect to the incident beam, for which the Q direction was either parallel or perpendicular to the pores for a scattering angle of 90 degrees . Diffuse neutron scattering at room temperature has shown that the aluminum oxide has amorphous structure and the polymer in the nanoporous matrix is partially crystallized. Concerning the dynamical behavior, for Q<1 A(-1), the spectra show Rouse-like motions indistinguishable from those in the bulk within the uncertainties. In the high-Q limit we observe a slowing down of the dynamics with respect to the bulk behavior that evidences an effect of confinement. This effect is more pronounced for molecular displacements perpendicular to the pore axis than for parallel displacements. Our results clearly rule out the strong corset effect proposed for this polymer from nuclear magnetic resonance (NMR) studies and can be rationalized by assuming that the interactions with the pore walls affect one to two adjacent monomer monolayers.

Abnormal strong burn-in degradation of highly efficient polymer solar cells caused by spinodal donor-acceptor demixing

The performance of organic solar cells is determined by the delicate, meticulously optimized bulk-heterojunction microstructure, which consists of finely mixed and relatively separated donor/acceptor regions. Here we demonstrate an abnormal strong burn-in degradation in highly efficient polymer solar cells caused by spinodal demixing of the donor and acceptor phases, which dramatically reduces charge generation and can be attributed to the inherently low miscibility of both materials. Even though the microstructure can be kinetically tuned for achieving high-performance, the inherently low miscibility of donor and acceptor leads to spontaneous phase separation in the solid state, even at room temperature and in the dark. A theoretical calculation of the molecular parameters and construction of the spinodal phase diagrams highlight molecular incompatibilities between the donor and acceptor as a dominant mechanism for burn-in degradation, which is to date the major short-time loss reducing the performance and stability of organic solar cells.

Cytoplasmic water and hydration layer dynamics in human red blood cells.

The dynamics of water in human red blood cells was measured with quasielastic incoherent neutron scattering in the temperature range between 290 and 320 K. Neutron spectrometers with time resolutions of 40, 13, and 7 ps were combined to cover time scales of bulk water dynamics to reduced mobility interfacial water motions. A major fraction of approximately 90% of cell water is characterized by a translational diffusion coefficient similar to bulk water. A minor fraction of approximately 10% of cellular water exhibits reduced dynamics. This slow water fraction was attributed to dynamically bound water on the surface of hemoglobin which accounts for approximately half of the hydration layer.

From Powder to Solution: Hydration Dependence of Human Hemoglobin Dynamics Correlated to Body Temperature

A transition in hemoglobin (Hb), involving partial unfolding and aggregation, has been shown previously by various biophysical methods. The correlation between the transition temperature and body temperature for Hb from different species, suggested that it might be significant for biological function. To focus on such biologically relevant human Hb dynamics, we studied the protein internal picosecond motions as a response to hydration, by elastic and quasielastic neutron scattering. Rates of fast diffusive motions were found to be significantly enhanced with increasing hydration from fully hydrated powder to concentrated Hb solution. In concentrated protein solution, the data showed that amino acid side chains can explore larger volumes above body temperature than expected from normal temperature dependence. The body temperature transition in protein dynamics was absent in fully hydrated powder, indicating that picosecond protein dynamics responsible for the transition is activated only at a sufficient level of hydration. A collateral result from the study is that fully hydrated protein powder samples do not accurately describe all aspects of protein picosecond dynamics that might be necessary for biological function.