This paper presents the multi-threading and internet message communication capabilities of Qu-Prolog. Message addresses are symbolic and the communications package provides high-level support that completely hides details of IP addresses and port numbers as well as the underlying TCP/IP transport layer. The combination of the multi-threads and the high level inter-thread message communications provide simple, powerful support for implementing internet distributed intelligent applications.
The π-helix located at the tetramer interface of two-component FMN-dependent reductases contributes to the structural divergence from canonical FMN-bound reductases within the NADPH:FMN reductase family. The π-helix in the SsuE FMN-dependent reductase of the alkanesulfonate monooxygenase system has been proposed to be generated by the insertion of a Tyr residue in the conserved α4-helix. Variants of Tyr118 were generated, and their X-ray crystal structures determined, to evaluate how these alterations affect the structural integrity of the π-helix. The structure of the Y118A SsuE π-helix was converted to an α-helix, similar to the FMN-bound members of the NADPH:FMN reductase family. Although the π-helix was altered, the FMN binding region remained unchanged. Conversely, deletion of Tyr118 disrupted the secondary structural properties of the π-helix, generating a random coil region in the middle of helix 4. Both the Y118A and Δ118 SsuE SsuE variants crystallize as a dimer. The MsuE FMN reductase involved in the desulfonation of methanesulfonates is structurally similar to SsuE, but the π-helix contains a His insertional residue. Exchanging the π-helix insertional residue of each enzyme did not result in equivalent kinetic properties. Structure-based sequence analysis further demonstrated the presence of a similar Tyr residue in an FMN-bound reductase in the NADPH:FMN reductase family that is not sufficient to generate a π-helix. Results from the structural and functional studies of the FMN-dependent reductases suggest that the insertional residue alone is not solely responsible for generating the π-helix, and additional structural adaptions occur to provide the altered gain of function.
Here we analyze the thermal runaway behavior of the 134 A-h GS Yuasa Li-ion cells (LSE134) using a novel large format fractional thermal runaway calorimeter and gas collection methodology. Results indicate an average total thermal runaway energy yield of 2.86 MJ, or 1.6 times the stored electrochemical energy; this follows an assertion commonly found in literature that energy yield scales linearly with capacity. The average fractional energy distribution was 2% through the cell body, 53% through the electrode winding, and 45% through the ejecta material and gases. Lot-to-lot variability in heat output was also identified. Additionally, it was found that an average of 416.6 SL of gas was generated which is approximately 3.1 L A-h-1. The exhaust gas was determined to be a mixture of carbon dioxide, methane, ethane, oxygen, hydrogen, and other short chain hydrocarbons. Carbon dioxide was the largest component by volume with a range of 41% to 52% followed by hydrogen which ranged from 28% to 41%. Larger cells appear to result in strong ejecta flow driven events with higher fractions of the total energy delivered via the flow as compared to smaller format Li-ion cells.
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