Physical properties of some novel nematic bimesogens for the flexoelectric effect

In a chiral nematic liquid crystal, the flexoelectric effect consists of a fast and linear coupling with an applied electric field. One difficulty to overcome is the unwinding of the helix that occurs at higher fields due to dielectric coupling. The use of bimesogens, which possess very low molecular dielectric anisotropy can improve flexoelectric characteristics. New bimesogen compounds have recently been synthesised that exhibit switching angles of 45° for applied fields of about 9 V.μm-1. In this paper, results from dielectric, electro-optic and dynamic light scattering measurements are reported for the new bimesogenic mixture. The dielectric anisotropy Δε changes sign with temperature and its values range between -0.2 and 0.3 for the temperature range studied. For Δε weakly positive, no electric field Freedericksz transition could be induced but Williams domains are observed instead. The large decrease in the bend elastic constant to viscosity coefficient ratio is attributed to a large increase in the bend viscosity coefficient. © 2001 OPA (Overseas Publishers Association) N.V. Published by license under the Gordon and Breach Science Publishers imprint, a member of the Taylor & Francis Group.

Geometrical properties and turbulent flame speed measurements in stationary premixed V-flames using direct numerical simulation

Three dimensional, fully compressible direct numerical simulations (DNS) of premixed turbulent flames are carried out in a V-flame configuration. The governing equations and the numerical implementation are described in detail, including modifications made to the Navier-Stokes Characteristic Boundary Conditions (NSCBC) to accommodate the steep transverse velocity and composition gradients generated when the flame crosses the boundary. Three cases, at turbulence intensities, u′/sL, of 1, 2, and 6 are considered. The influence of the flame holder on downstream flame properties is assessed through the distributions of the surface-conditioned displacement speed, curvature and tangential strain rates, and compared to data from similarly processed planar flames. The distributions are found to be indistinguishable from planar flames for distances greater than about 17δth downstream of the flame holder, where δth is the laminar flame thermal thickness. Favre mean fields are constructed, and the growth of the mean flame brush is found to be well described by simple Taylor type diffusion. The turbulent flame speed, sT is evaluated from an expression describing the propagation speed of an isosurface of the mean reaction progress variable c̃ in terms of the imbalance between the mean reactive, diffusive, and turbulent fluxes within the flame brush. The results are compared to the consumption speed, sC, calculated from the integral of the mean reaction rate, and to the predictions of a recently developed flame speed model (Kolla et al., Combust Sci Technol 181(3):518-535, 2009). The model predictions are improved in all cases by including the effects of mean molecular diffusion, and the overall agreement is good for the higher turbulence intensity cases once the tangential convective flux of c̃ is taken into account. © 2010 Springer Science+Business Media B.V.

Effect of the interplay between protein and surface on the properties of adsorbed protein layers.

Although protein adsorption to surface is a common phenomenon, investigation of the process is challenging due to the complexity of the interplay between external factors, protein and surface properties. Therefore experimental approaches have to measure the properties of adsorbed protein layers with high accuracy in order to achieve a comprehensive description of the process. To this end, we used a combination of two biosensing techniques, dual polarization interferometry and quartz crystal microbalance with dissipation. From this, we are able to extract surface coverage values, layer structural parameters, water content and viscoelastic properties to examine the properties of protein layers formed at the liquid/solid interface. Layer parameters were examined upon adsorption of proteins of varying size and structural properties, on surfaces with opposite polarity. We show that "soft" proteins such as unfolded α-synuclein and high molecular weight albumin are highly influenced by the surface polarity, as they form a highly diffuse and hydrated layer on the hydrophilic silica surface as opposed to the denser, less hydrated layer formed on a hydrophobic methylated surface. These layer properties are a result of different orientations and packing of the proteins. By contrast, lysozyme is barely influenced by the surface polarity due to its intrinsic structural stability. Interestingly, we show that for a similar molecular weight, the unfolded α-synuclein forms a layer with the highest percentage of solvation not related to surface coverage but resulting from the highest water content trapped within the protein. Together, these data reveal a trend in layer properties highlighting the importance of the interplay between protein and surface for the design of biomaterials.

Effect of the interplay between protein and surface on the properties of adsorbed protein layers

Although protein adsorption to surface is a common phenomenon, investigation of the process is challenging due to the complexity of the interplay between external factors, protein and surface properties. Therefore experimental approaches have to measure the properties of adsorbed protein layers with high accuracy in order to achieve a comprehensive description of the process. To this end, we used a combination of two biosensing techniques, dual polarization interferometry and quartz crystal microbalance with dissipation. From this, we are able to extract surface coverage values, layer structural parameters, water content and viscoelastic properties to examine the properties of protein layers formed at the liquid/solid interface. Layer parameters were examined upon adsorption of proteins of varying size and structural properties, on surfaces with opposite polarity. We show that "soft" proteins such as unfolded α-synuclein and high molecular weight albumin are highly influenced by the surface polarity, as they form a highly diffuse and hydrated layer on the hydrophilic silica surface as opposed to the denser, less hydrated layer formed on a hydrophobic methylated surface. These layer properties are a result of different orientations and packing of the proteins. By contrast, lysozyme is barely influenced by the surface polarity due to its intrinsic structural stability. Interestingly, we show that for a similar molecular weight, the unfolded α-synuclein forms a layer with the highest percentage of solvation not related to surface coverage but resulting from the highest water content trapped within the protein. Together, these data reveal a trend in layer properties highlighting the importance of the interplay between protein and surface for the design of biomaterials. © 2014 The Authors.