33 research outputs found

    Ca4_{4}YO(BO3_{3})3: Optical frame wavelength dependence, second harmonic generation and dispersion equations

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    We report that the optical frame orientation is wavelength independent over the entire transmission range of the nonlinear monoclinic crystal Ca4_{4}YO(BO3_{3})3_{3} (YCOB). We used a new method based on internal conical refraction associated with X-rays diffraction using a single crystal cut as a sphere. Direct measurements phase matching angles of second harmonic generation (SHG) were performed in the principal planes of the spherical crystal for fundamental wavelengths up to 3.5 μ\mum, while three absorption peaks have been measured above 2.4 μ\mum. By fitting all data simultaneously, we found new dispersion equations of the refractive indices of YCOB which are valid in its whole transmission domain

    Influence of ACE-inhibition on salt-mediated worsening of pulmonary gas exchange in heart failure

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    In congestive heart failure (CHF), pulmonary gas exchange, as evaluated by carbon monoxide diffusion (DLCO), is impaired. ACE-inhibition improves DLCO. Infusion of saline worsens DLCO, because of upregulated sodium and water transport to the alveolar interstitium, which thickens the alveolar-capillary interface and lengthens the diffusion path for gas exchange. We investigated whether enalapril can readjust the capillary permeability to sodium

    Understanding cooperative protein adsorption events at the microscopic scale: a comparison between experimental data and Monte Carlo simulations

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    Cooperative effects play a vital role in protein adsorption events on biological interfaces. Despite a number of studies in this field molecular adsorption mechanisms that include cooperativity are still under debate. In this work we use a Monte Carlo-type simulation to explore the microscopic details behind cooperative protein adsorption. The simulation was designed to implement our previously proposed mechanism through which proteins are not necessarily rejected if they approach the surface to an occupied region. Instead, we suggest that proteins can be tracked laterally for a certain distance due to the influence of preadsorbed proteins in order to reach the nearest available binding site. The simulation results were compared with experimental data obtained by using the supercritical angle fluorescence (SAF) microscopy technique. It was found that the tracking distance may be up to 2.5 times the protein’s diameter depending on the investigated system. The general validity of this tracking mechanism is supported by a number of linear or upward concave adsorption kinetics reported in the literature which are consistent with our simulation results. Furthermore, the self-organization of proteins adsorbing under cooperative conditions on the surface is shown to necessarily cause density inhomogeneities in the surface distribution of proteins which is also in agreement with experimental observations

    What governs protein adsorption and immobilization at a charged solid surface?

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    The adsorption alien egg white lysozyme at a model charged surface is studied using fully atomistic molecular dynamics simulations. The simulations are performed over a 90 ns time scale which is sufficient to observe rotational and translational steps in the adsorption process. Electrostatics is found to play a key role in guiding the protein to the favorable binding orientation with the N,C-terminal face against the substrate. However, full immobilization appears to only occur through the strong interaction of Arg128 with the surface, facilitated by the protein's flexibility at the terminal face. Simulated mutation at this residue confirms its crucial role. This work demonstrates that electrostatics alone might not be sufficient to guide the development of material systems that exploit protein adsorption and immobilization
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