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Juan M. Lujano-Rojas,Ghassan Zubi,Rodolfo Dufo-López,José L. Bernal-Agustín,José L. Atencio-Guerra,João P. S. Catalão 한국CDE학회 2020 Journal of computational design and engineering Vol.7 No.2
This paper presents a methodology for the optimal placement and sizing of reactive power compensation devices in a distribution system (DS) with distributed generation. Quasi-static time series is embedded in an optimization method based on a genetic algorithm to adequately represent the uncertainty introduced by solar photovoltaic generation and electricity demand and its effect on DS operation. From the analysis of a typical DS, the reactive power compensation rating power results in an increment of 24.9% when compared to the classical genetic algorithm model. However, the incorporation of quasi-static time series analysis entails an increase of 26.8% on the computational time required.
Zhu, Qiankun,Zhu, Mengli,Fan, Gaotao,Zou, Jiaxin,Feng, Peichun,Liu, Zubi,Wang, Wanjun Korean Chemical Society 2014 Bulletin of the Korean Chemical Society Vol.35 No.1
Coptis chinensis 3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase (HOMT), an essential enzyme in the berberine biosynthetic pathway, catalyzes the methylation of 3'-hydroxy-N-methylcoclaurine (HMC) producing reticuline. A 3D model of HOMT was constructed by homology modeling and further subjected to docking with its ligands and molecular dynamics simulations. The 3D structure of HOMT revealed unique structural features which permitted the methylation of HMC. The methylation of HMC was proposed to proceed by deprotonation of the 4'-hydroxyl group via His257 and Asp258 of HOMT, followed by a nucleophilic attack on the SAM-methyl group resulting in reticuline. HOMT showed high substrate specificity for methylation of HMC. The study evidenced that Gly117, Thr312 and Asp258 in HOMT might be the key residues for orienting substrate for specific catalysis.
Qiankun Zhu,Mengli Zhu,Gaotao Fan,Jiaxin Zou,Peichun Feng,Zubi Liu,Wanjun Wang 대한화학회 2014 Bulletin of the Korean Chemical Society Vol.35 No.1
Coptis chinensis 3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase (HOMT), an essential enzyme in the berberine biosynthetic pathway, catalyzes the methylation of 3'-hydroxy-N-methylcoclaurine (HMC) producing reticuline. A 3D model of HOMT was constructed by homology modeling and further subjected to docking with its ligands and molecular dynamics simulations. The 3D structure of HOMT revealed unique structural features which permitted the methylation of HMC. The methylation of HMC was proposed to proceed by deprotonation of the 4'-hydroxyl group via His257 and Asp258 of HOMT, followed by a nucleophilic attack on the SAM-methyl group resulting in reticuline. HOMT showed high substrate specificity for methylation of HMC. The study evidenced that Gly117, Thr312 and Asp258 in HOMT might be the key residues for orienting substrate for specific catalysis.