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DFT Analysis of the Adsorption of Methyl Nitrate on Al2O3 Surfaces
Yan-qun Wang,Xiu-fen Yan,Wei Xiao,You-xiang Shao 대한화학회 2017 Bulletin of the Korean Chemical Society Vol.38 No.6
The adsorption of the energetic molecule methyl nitrate (CH3ONO2) on α-Al2O3(0001) and γ-Al2O3(110) surfaces was investigated using first-principles calculations based on density functional theory and the generalized gradient approximation. We found that CH3ONO2 approaches the two surfaces by either the oxygen connected with carbon atom or an oxygen atom of the nitro group; however, the former interaction is more stable. If CH3ONO2 approaches the surface through the oxygen atom of the nitro group, the adsorption is non-dissociative; while it is nearly dissociative if CH3ONO2 adsorbs on the surface via the oxygen connected with carbon atom and a surface tri-coordinated Al atom. Moreover, the dissociation trend on the γ-Al2O3(110) surface is more pronounced. In addition, the adsorption of CH3ONO2 on the γ-Al2O3(110) surface is more favorable. Finally, although strong interactions exist between CH3ONO2 and the surfaces, the structures of the alumina films are not affected by the adsorption of CH3ONO2.
Zhan-qing Zhang,Yan-bing Wang,,Wei Lu,,Dan-ping Liu,,Bi-sheng Shi,,Xiao-nan Zhang,,Dan Huang,,Xiu-fen Li,,Xin-lan Zhou,,Rong-rong Ding, 대한진단검사의학회 2019 Annals of Laboratory Medicine Vol.39 No.1
Background: We examined changes in hepatitis B core-related antigen (HBcrAg) during the four sequential phases of chronic hepatitis B virus (HBV) infection: hepatitis B e antigen (HBeAg)-positive chronic infection (EPCI) and hepatitis (EPCH), followed by HBeAg-negative chronic infection (ENCI) and hepatitis (ENCH). We compared the performance of serum HBcrAg, hepatitis B surface antigen (HBsAg), and HBV DNA in predicting EPCH and ENCH.
( Xing Long Wang ),( Li Liu ),( Si Xiu Liu ),( Xiao Qing Sun ),( Zhong Xiang Deng ),( Yan Pi ),( Xiao Fen Sun ),( Ke Xuan Tang ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.5
A new CRT binding factor (CBF) gene designated Cbcbf25 was cloned from Capsella bursa pastoris, a wild grass, by the rapid amplification of cDNA ends (RACE). The full-length cDNA of Cbcbf25 was 898 bp with a 669 bp open reading frame (ORF) encoding a putative DRE/CRT (LTRE)-binding protein of 223 amino acids. The predicted CbCBF25 protein contained a potential nuclear localization signal (NLS) in its N-terminal region followed by an AP2 DNA-binding motif and a possible acidic activation domain in the C-terminal region. Bioinformatic analysis revealed that Cbcbf25 has a high level of similarity with other CBF genes like cbfl, cbf2, and cbf3 from Arabidopsis thaliana, and Bncbf5, Bncbf7, Bncbfl6, and Bncbfl7 from Brassica napus. A cold acclimation assay showed that Cbcbf25 was expressed immediately after cold triggering, but this expression was transient, suggesting that it concerns cold acclimation. Our study implies that Cbcbf25 is an analogue of other CBF genes and may participate in cold-response, by for example, controlling the expression of cold-regulated genes or increasing the freezing tolerance of plants.