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RISS 인기검색어
- 검색키워드
- 저자 : Changjiang Guo (검색결과 4 건)
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Nonlinear wind-induced instability of orthotropic plane membrane structures
Changjiang Liu,Feng Ji,Zhoulian Zheng,Yuyou Wu,Jianjun Guo 한국풍공학회 2017 Wind and Structures, An International Journal (WAS Vol.25 No.5
he nonlinear aerodynamic instability of a tensioned plane orthotropic membrane structure is theoretically investigated in this paper. The interaction governing equation of wind-structure coupling is established by the Von Kármán\'s large amplitude theory and the D\'Alembert\'s principle. The aerodynamic force is determined by the potential flow theory of fluid mechanics and the thin airfoil theory of aerodynamics. Then the interaction governing equation is transformed into a second order nonlinear differential equation with constant coefficients by the Bubnov-Galerkin method. The critical wind velocity is obtained by judging the stability of the second order nonlinear differential equation. From the analysis of examples, we can conclude that it\'s of great significance to consider the orthotropy and geometrical nonlinearity to prevent the aerodynamic instability of plane membrane structures; we should comprehensively consider the effects of various factors on the design of plane membrane structures; and the formula of critical wind velocity obtained in this paper provides a more accurate theoretical solution for the aerodynamic stability of the plane membrane structures than the previous studies.
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Nonlinear wind-induced instability of orthotropic plane membrane structures
Liu, Changjiang,Ji, Feng,Zheng, Zhoulian,Wu, Yuyou,Guo, Jianjun Techno-Press 2017 Wind and Structures, An International Journal (WAS Vol.25 No.5
The nonlinear aerodynamic instability of a tensioned plane orthotropic membrane structure is theoretically investigated in this paper. The interaction governing equation of wind-structure coupling is established by the Von $K\acute{a}rm\acute{a}n's$ large amplitude theory and the D'Alembert's principle. The aerodynamic force is determined by the potential flow theory of fluid mechanics and the thin airfoil theory of aerodynamics. Then the interaction governing equation is transformed into a second order nonlinear differential equation with constant coefficients by the Bubnov-Galerkin method. The critical wind velocity is obtained by judging the stability of the second order nonlinear differential equation. From the analysis of examples, we can conclude that it's of great significance to consider the orthotropy and geometrical nonlinearity to prevent the aerodynamic instability of plane membrane structures; we should comprehensively consider the effects of various factors on the design of plane membrane structures; and the formula of critical wind velocity obtained in this paper provides a more accurate theoretical solution for the aerodynamic stability of the plane membrane structures than the previous studies.
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Comparative Study of the marR Genes within the Family Enterobacteriaceae
Dan Wang,Changjiang Guo,Longjiang Gu,Xiaohui Zhang 한국미생물학회 2014 The journal of microbiology Vol.52 No.6
marR genes are members of an ancient family originallyidentified in Escherichia coli. This family is widely distributedin archaea and bacteria. Homologues of this family have aconserved winged helix fold. MarR proteins are involved innon-specific resistance systems conferring resistance to multipleantibiotics. Extensive studies have shown the importanceof MarR proteins in physiology and pathogenicity inEnterobacteria, but little is known about their origin or evolution. In this study, all the marR genes in 43 enterobacterialgenomes representing 14 genera were identified, and the phylogeneticrelationships and genetic parameters were analyzed. Several major findings were made. Three conserved marRgenes originated earlier than Enterobacteriaceae and a genelossevent was found to have taken place in Yersinia pestisAntiqua. Three functional genes, rovA, hor, and slyA, werefound to be clear orthologs among Enterobacteriaceae. Thecopy number of marR genes in Enterobacteriaceae was foundto vary from 2 to 11. These marR genes exhibited a faster rateof nucleotide substitution than housekeeping genes did. Specifically, the regions of marR domain were found to besubject to strong purifying selection. The phylogenetic relationshipand genetic parameter analyses were consistentwith conservation and specificity of marR genes. These dualcharacters helped MarR to maintain a conserved bindingmotif and variable C-terminus, which are important to adaptiveresponses to a number of external stimuli in Enterobacteriaceae.
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Shuang Wang,Jingmin Gu,Meng Lv,Zhimin Guo,Guangmou Yan,Ling Yu,Chongtao Du,Xin Feng,Wenyu Han,Changjiang Sun,Liancheng Lei 한국미생물학회 2017 The journal of microbiology Vol.55 No.5
Bacteriophage endolysin is one of the most promising antibioticsubstitutes, but in Gram-negative bacteria, the outermembrane prevents the lysin from hydrolyzing peptidoglycansand blocks the development of lysin applications. Theprime strategy for new antibiotic substitutes is allowing lysinto access the peptidoglycan from outside of the bacteria byreformation of the lysin. In this study, the novel Escherichiacoli (E. coli) phage lyase lysep3, which lacks outside-in catalyticability, was fused with the N-terminal region of theBacillus amyloliquefaciens lysin including its cell wall bindingdomain D8 through the best manner of protein fusionbased on the predicted tertiary structure of lysep3-D8 to obtainan engineered lysin that can lyse bacteria from the outside. Our results showed that lysep3-D8 could lyse both Gramnegativeand Gram-positive bacteria, whereas lysep3 and D8have no impact on bacterial growth. The MIC of lysep3-D8on E. coli CVCC1418 is 60 μg/ml; lysep3-D8 can inhibit thegrowth of bacteria up to 12 h at this concentration. The bactericidalspectrum of lysep3-D8 is broad, as it can lyse of allof 14 E. coli strains, 3 P. aeruginosa strains, 1 Acinetobacterbaumannii strain, and 1 Streptococcus strain. Lysep3-D8 hassufficient bactericidal effects on the 14 E. coli strains testedat the concentration of 100 μg/ml. The cell wall binding domainof the engineered lysin can destroy the integrity of theouter membrane of bacteria, thus allowing the catalytic domainto reach its target, peptidoglycan, to lyse the bacteria. Lysep3-D8 can be used as a preservative in fodder to benefitthe health of animals. The method we used here proved to bea successful exploration of the reformation of phage lysin.
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