136 research outputs found

    The Effect of the Pairing Interaction on the Energies of Isobar Analog Resonances in 112124^{112-124}Sb and Isospin Admixture in 100124^{100-124}Sn Isotopes

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    In the present study, the effect of the pairing interaction and the isovector correlation between nucleons on the properties of the isobar analog resonances (IAR) in 112124^{112-124}Sb isotopes and the isospin admixture in 100124^{100-124}Sn isotopes is investigated within the framework of the quasiparticle random phase approximation (QRPA). The form of the interaction strength parameter is related to the shell model potential by restoring the isotopic invariance of the nuclear part of the total Hamiltonian. In this respect, the isospin admixtures in the 100124^{100-124}Sn isotopes are calculated, and the dependence of the differential cross section and the volume integral JFJ_{F} for the Sn(3^{3}He,t)Sb reactions at E(3^{3}He)=200=200 MeV occurring by the excitation of IAR on mass number A is examined. Our results show that the calculated value for the isospin mixing in the 100^{100}Sn isotope is in good agreement with Colo et al.'s estimates (45(4-5%), and the obtained values for the volume integral change within the error range of the value reported by Fujiwara et al. (53±\pm5 MeV fm3^{3}). Moreover, it is concluded that although the differential cross section of the isobar analog resonance for the (3^{3}He,t) reactions is not sensitive to pairing correlations between nucleons, a considerable effect on the isospin admixtures in NZN\approx Z isotopes can be seen with the presence of these correlations.Comment: 16 pages, 5 EPS figures and 2 tables, Late

    Visualizing Escherichia coli Sub-Cellular Structure Using Sparse Deconvolution Spatial Light Interference Tomography

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    Studying the 3D sub-cellular structure of living cells is essential to our understanding of biological function. However, tomographic imaging of live cells is challenging mainly because they are transparent, i.e., weakly scattering structures. Therefore, this type of imaging has been implemented largely using fluorescence techniques. While confocal fluorescence imaging is a common approach to achieve sectioning, it requires fluorescence probes that are often harmful to the living specimen. On the other hand, by using the intrinsic contrast of the structures it is possible to study living cells in a non-invasive manner. One method that provides high-resolution quantitative information about nanoscale structures is a broadband interferometric technique known as Spatial Light Interference Microscopy (SLIM). In addition to rendering quantitative phase information, when combined with a high numerical aperture objective, SLIM also provides excellent depth sectioning capabilities. However, like in all linear optical systems, SLIM's resolution is limited by diffraction. Here we present a novel 3D field deconvolution algorithm that exploits the sparsity of phase images and renders images with resolution beyond the diffraction limit. We employ this label-free method, called deconvolution Spatial Light Interference Tomography (dSLIT), to visualize coiled sub-cellular structures in E. coli cells which are most likely the cytoskeletal MreB protein and the division site regulating MinCDE proteins. Previously these structures have only been observed using specialized strains and plasmids and fluorescence techniques. Our results indicate that dSLIT can be employed to study such structures in a practical and non-invasive manner

    Super-resolution:A comprehensive survey

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    Affinity binding of antibodies to supermacroporous cryogel adsorbents with immobilized protein A for removal of anthrax toxin protective antigen

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    Polymeric cryogels are efficient carriers for the immobilization of biomolecules because of their unique macroporous structure, permeability, mechanical stability and different surface chemical functionalities. The aim of the study was to demonstrate the potential use of macroporous monolithic cryogels for biotoxin removal using anthrax toxin protective antigen (PA), the central cell-binding component of the anthrax exotoxins, and covalent immobilization of monoclonal antibodies. The affinity ligand (protein A) was chemically coupled to the reactive hydroxyl and epoxy-derivatized monolithic cryogels and the binding efficiencies of protein A, monoclonal antibodies to the cryogel column were determined. Our results show differences in the binding capacity of protein A as well as monoclonal antibodies to the cryogel adsorbents caused by ligand concentrations, physical properties and morphology of surface matrices. The cytotoxicity potential of the cryogels was determined by an in vitro viability assay using V79 lung fibroblast as a model cell and the results reveal that the cryogels are non-cytotoxic. Finally, the adsorptive capacities of PA from phosphate buffered saline (PBS) were evaluated towards a non-glycosylated, plant-derived human monoclonal antibody (PANG) and a glycosylated human monoclonal antibody (Valortim®), both of which were covalently attached via protein A immobilization. Optimal binding capacities of 108 and 117 mg/g of antibody to the adsorbent were observed for PANG attached poly(acrylamide-allyl glycidyl ether) [poly(AAm-AGE)] and Valortim® attached poly(AAm-AGE) cryogels, respectively, This indicated that glycosylation status of Valortim® antibody could significantly increase (8%) its binding capacity relative to the PANG antibody on poly(AAm-AGE)-protien-A column (p < 0.05). The amounts of PA which remained in the solution after passing PA spiked PBS through PANG or Valortim bound poly(AAm-AGE) cryogel were significantly (p < 0.05) decreased relative to the amount of PA remained in the solution after passing through unmodified as well as protein A modified poly(AAm-AGE) cryogel columns, indicates efficient PA removal from spiked PBS over 60 min of circulation. The high adsorption capacity towards anthrax toxin PA of the cryogel adsorbents indicated potential application of these materials for treatment of Bacillus anthracis infection

    PCOS AND AMH

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    &lt;p&gt;Polycystic ovary syndrome (PCOS) is one of the most common endocrine disorders among reproductive-aged women and affects 10–15% of them (Neven, A.C.H; Laven, J; Teede, H.J; Boyle, J.A.;) (Bozdag, Mumusoglu, Zengin , Karabulut, &amp; Yildiz).&nbsp;&lt;/p&gt

    Implementation of a neurophysiologically-based coding strategy for the cochlear implant

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    Refractory State Coding (RSC) is a new coding strategy based on a functional model of the stimulated neural population. Our hypothesis is that RSC stimulation would convey the information contained in acoustic signals more effectively, improving sound perception and hearing performance for speech in noise and music. Two main factors that RSC takes into account are channel interaction [1] and refractory properties [2] of the stimulated neural population. They can be characterized by electrophysiological measurements of the evoked compound action potential (ECAP) using “spread of excitation” (SoE) and “recovery function” characterization paradigms respectively [3]. Using this information, for a given stimulus sequence, it is possible to calculate the refractory state of each stimulation site at any given time. In RSC, the stimulus is shaped according to the refractory states of stimulation sites. The spectral representation of the input sound is weighted by the refractory recovery information as well as the electric field distribution function before the next stimulus is selected. The Nucleus 24 and Nucleus Freedom family of cochlear implants incorporate Neural Response Telemetry (NRT) circuitry which is able to conveniently measure the ECAP from the implanted intracochlear electrodes, allowing the model to be custom-fitted to a patient. A software implementation of the standard ACE strategy for the Nucleus Cochlear Implant system is available in the Nucleus Matlab Toolbox. We implemented the RSC strategy in a compatible fashion in Matlab
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