1,663 research outputs found

    The Mirror and the Porthole

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    The Jeffersonian Gunboat Navy

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    Stability and Reversibility of Lithium Borohydrides Doped by Metal Halides and Hydrides

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    In an effort to develop reversible metal borohydrides with high hydrogen storage capacities and low dehydriding temperature, doping LiBH4 with various metal halides and hydrides has been conducted. Several metal halides such as TiCl3, TiF3, and ZnF2 effectively reduced the dehydriding temperature through a cation exchange interaction. Some of the halide doped LiBH4 are partially reversible. The LiBH4 + 0.1TiF3 desorbed 3.5 wt % and 8.5 wt % hydrogen at 150 and 450 °C, respectively, with subsequent reabsorption of 6 wt % hydrogen at 500 °C and 70 bar observed. XRD and NMR analysis of the rehydrided samples confirmed the reformation of LiBH4. The existence of the (B12H12)−2 species in dehydrided and rehydrided samples gives insight into the resultant partial reversibility. A number of other halides, MgF2, MgCl2, CaCl2, SrCl2, and FeCl3, did not reduce the dehydriding temperature of LiBH4 significantly. XRD and TGA-RGA analyses indicated that an increasing proportion of halides such as TiCl3, TiF3, and ZnCl2 from 0.1 to 0.5 mol makes lithium borohydrides less stable and volatile. Although the less stable borohydrides such as LiBH4 + 0.5TiCl3, LiBH4 + 0.5TiF3, and LiBH4 + 0.5ZnCl2 release hydrogen at room temperature, they are not reversible due to unrecoverable boron loss caused by diborane emission. In most cases, doping that produced less stable borohydrides also reduced the reversible hydrogen uptake. It was also observed that halide doping changed the melting points and reduced air sensitivity of lithium borohydrides

    Signal distortion from microelectrodes in clinical EEG acquisition systems

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    Many centers are now using high-density microelectrodes during traditional intracranial electroencephalography (iEEG) both for research and clinical purposes. These microelectrodes are FDA-approved and integrate into clinical EEG acquisition systems. However, the electrical characteristics of these electrodes are poorly described and clinical systems were not designed to use them; thus, it is possible that this shift into clinical practice could have unintended consequences. In this study, we characterized the impedance of over 100 commercial macro- and microelectrodes using electrochemical impedance spectroscopy (EIS) to determine how electrode properties could affect signal acquisition and interpretation. The EIS data were combined with the published specifications of several commercial EEG systems to design digital filters that mimic the behavior of the electrodes and amplifiers. These filters were used to analyze simulated brain signals that contain a mixture of characteristic features commonly observed in iEEG. Each output was then processed with several common quantitative EEG measurements. Our results show that traditional macroelectrodes had low impedances and produced negligible distortion of the original signal. Brain tissue and electrical wiring also had negligible filtering effects. However, microelectrode impedances were much higher and more variable than the macroelectrodes. When connected to clinical amplifiers, higher impedance electrodes produced considerable distortion of the signal at low frequencies (<60 Hz), which caused significant changes in amplitude, phase, variance and spectral band power. In contrast, there were only minimal changes to the signal content for frequencies above 100 Hz. In order to minimize distortion with microelectrodes, we determined that an acquisition system should have an input impedance of at least 1 GΩ, which is much higher than most clinical systems. These results show that it is critical to account for variations in impedance when analyzing EEG from different-sized electrodes. Data from microelectrodes may yield misleading results unless recorded with high-impedance amplifiers.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/98632/1/1741-2552_9_5_056007.pd

    Temporal pattern of africanization in a feral honeybee population from Texas inferred from mitochondrial DNA

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    The invasion of Africanized honeybees (Apis mellifera L.) in the Americas provides a window of opportunity to study the dynamics of secondary contact of subspecies of bees that evolved in allopatry in ecologically distinctive habitats of the Old World. We report here the results of an 11-year mitochondrial DNA survey of a feral honeybee population from southern United States (Texas). The mitochondrial haplotype (mitotype) frequencies changed radically during the 11-year study period. Prior to immigration of Africanized honeybees, the resident population was essentially of eastern and western European maternal ancestry. Three years after detection of the first Africanized swarm there was a mitotype turnover in the population from predominantly eastern European to predominantly A. m. scutellata (ancestor of Africanized honeybees). This remarkable change in the mitotype composition coincided with arrival of the parasitic mite Varroa destructor, which was likely responsible for severe losses experienced by colonies of European ancestry. From 1997 onward the population stabilized with most colonies of A. m. scutellata maternal origin.PRODEP II - Medida 5/Acção 5.

    The Ursinus Weekly, November 19, 1956

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    Noted Japanese law professor to address UC Forum • Our town given Nov. 15, 16 and 17 • French Club views slides on south France • Yale pledges aid: $2,000 to Hungary student refugees • Frosh members of MSGA installed • ZX party held Saturday • Help Hungary fund sponsored by Weekly; Ends Wednesday • C-T senior class to present Fog island • Chess Club match • Cooperation and revision topics of MS-WSGA meeting • Y hears noted sociologist speak • YM-YW sponsors panel discussion on frosh customs • High society is Fall prom theme • Dumb frosh!! • Editorial: They gave all • Big haircut • Clique: A problem for student activities • Play review: Our town • Belles unbeaten streak stopped by E. Stroudsburg, 1-0; Beat Penn 4-0 • Season bows out as gridders drop fourth to Indians, 33-6; End 3-4-1 • Booters hold F&M to 0-0 tie; Finish with 2-5-3 slate • Dolman releases frosh statistics • Pre-meds to hear talk on internal medicine • Great prints exhibited at Phila. art museum • Work on new dorms progresses • Ursinus grad becomes U.S. Navy carrier pilot • Y presidents pinned • Chi Alpha hears talk on Greek, Hebrew ideas • Ursinus grad in Francehttps://digitalcommons.ursinus.edu/weekly/1416/thumbnail.jp

    Structure of the Herpes Simplex Virus Capsid: Peptide A862-H880 of the Major Capsid Protein Is Displayed on the Rim of the Capsomer Protrusions

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    AbstractThe herpes simplex virus-1 (HSV-1) capsid shell has 162 capsomers arranged on aT= 16 icosahedral lattice. The major capsid protein, VP5 (MW = 149,075) is the structural component of the capsomers. VP5 is an unusually large viral capsid protein and has been shown to consist of multiple domains. To study the conformation of VP5 as it is folded into capsid protomers, we identified the sequence recognized by a VP5-specific monoclonal antibody and localized the epitope on the capsid surface by cryoelectron microscopy and image reconstruction. The epitope of mAb 6F10 was mapped to residues 862–880 by immunoblotting experiments performed with (1) proteolytic fragments of VP5, (2) GST-fusion proteins containing VP5 domains, and (3) synthetic VP5 peptides. As visualized in a three-dimensional density map of 6F10-precipitated capsids, the antibody was found to bind at sites on the outer surface of the capsid just inside the openings of thetrans-capsomeric channels. We conclude that these sites are occupied by peptide 862–880 in the mature HSV-1 capsid
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