Oxide Materials for Thermochemical CO2 and H2O-Splitting Using Concentrated Solar Energy
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Nature Physics
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Metallography, Microstructure, and Analysis
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Physical review
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Public Interest Report (by the Federation of American Scientists)
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Applied Physics Letters
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This presentation discusses some of the terminology used to model and simulate scenarios for military training.
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Journal of Alloys and Compounds
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While the 2011 National Electrical Codeª (NEC) only requires series arc-fault protection, some arc-fault circuit interrupter (AFCI) manufacturers are designing products to detect and mitigate both series and parallel arc-faults. Sandia National Laboratories (SNL) has extensively investigated the electrical differences of series and parallel arc-faults and has offered possible classification and mitigation solutions. As part of this effort, Sandia National Laboratories has collaborated with MidNite Solar to create and test a 24-string combiner box with an AFCI which detects, differentiates, and de-energizes series and parallel arc-faults. In the case of the MidNite AFCI prototype, series arc-faults are mitigated by opening the PV strings, whereas parallel arc-faults are mitigated by shorting the array. A range of different experimental series and parallel arc-fault tests with the MidNite combiner box were performed at the Distributed Energy Technologies Laboratory (DETL) at SNL in Albuquerque, NM. In all the tests, the prototype de-energized the arc-faults in the time period required by the arc-fault circuit interrupt testing standard, UL 1699B. The experimental tests confirm series and parallel arc-faults can be successfully mitigated with a combiner box-integrated solution.
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Ion channel proteins regulate complex patterns of cellular electrical activity and ionic signaling. Certain K+ channels play an important role in immunological biodefense mechanisms of adaptive and innate immunity. Most ion channel proteins are oligomeric complexes with the conductive pore located at the central subunit interface. The long-term activity of many K+ channel proteins is dependent on the concentration of extracellular K+; however, the mechanism is unclear. Thus, this project focused on mechanisms underlying structural stability of tetrameric K+ channels. Using KcsA of Streptomyces lividans as a model K+ channel of known structure, the molecular basis of tetramer stability was investigated by: 1. Bioinformatic analysis of the tetramer interface. 2. Effect of two local anesthetics (lidocaine, tetracaine) on tetramer stability. 3. Molecular simulation of drug docking to the ion conduction pore. The results provide new insights regarding the structural stability of K+ channels and its possible role in cell physiology.
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