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R. Grosseuvres A. Comandini A. Bentaib N. Chaumeix 《Proceedings of the Combustion Institute》2019,37(2):1537-1546
The present work reports new experimental and numerical results of the combustion properties of hydrogen based mixtures diluted by nitrogen and steam. Spherical expanding flames have been studied in a spherical bomb over a large domain of equivalence ratios, initial temperatures and dilutions at an initial pressure of 100 kPa (Tini = 296, 363, 413 K; N2/O2 = 3.76, 5.67, 9; %Steam = 0, 20, 30). From these experiments, the laminar flame speed , the Markstein length L’, the activation energy Ea and the Zel'dovich β number have been determined. These parameters were also simulated using COSILAB® in order to verify the validity of the Mével et al. [1] detailed kinetic mechanism. Other parameters as the laminar flame thickness δ and the effective Lewis number Leeff were also simulated. These new results aim at providing an extended database that will be very useful in the hydrogen combustion hazard assessment for nuclear reactor power plant new design. 相似文献
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The serine protease, DegP exhibits proteolytic and chaperone activities, essential for cellular protein quality control and normal cell development in eukaryotes. The P. falciparum DegP is essential for the parasite survival and required to combat the oscillating thermal stress conditions during the infection, protein quality checks and protein homeostasis in the extra-cytoplasmic compartments, thereby establishing it as a potential target for drug development against malaria. Previous studies have shown that diisopropyl fluorophosphate (DFP) and the peptide SPMFKGV inhibit E. coli DegP protease activity. To identify novel potential inhibitors specific to PfDegP allosteric and the catalytic binding sites, we performed a high throughput in silico screening using Malaria Box, Pathogen Box, Maybridge library, ChEMBL library and the library of FDA approved compounds. The screening helped identify five best binders that showed high affinity to PfDegP allosteric (T0873, T2823, T2801, , CD00811) and the catalytic binding site (T0078L, T1524, T2328, BTB11534 and 552691). Further, molecular dynamics simulation analysis revealed RJC02337, BTB11534 as the best hits forming a stable complex. WaterMap and electrostatic complementarity were used to evaluate the novel bio-isosteric chemotypes of RJC02337, that led to the identification of 231 chemotypes that exhibited better binding affinity. Further analysis of the top 5 chemotypes, based on better binding affinity, revealed that the addition of electron donors like nitrogen and sulphur to the side chains of butanoate group are more favoured than the backbone of butanoate group. In a nutshell, the present study helps identify novel, potent and Plasmodium specific inhibitors, using high throughput in silico screening and bio-isosteric replacement, which may be experimentally validated. RJC02337相似文献