• Title/Summary/Keyword: crystal cells

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Study on Surface Temperature Change of PV Module Installed on Green Roof System and Non-green Roof System (옥상녹화와 비 옥상녹화 평지붕에 설치 된 PV모듈의 표면온도 변화 고찰)

  • Yoo, Dong-Chul;Lee, Eung-Jik;Lee, Doo-Ho
    • 한국태양에너지학회:학술대회논문집
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    • 2011.11a
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    • pp.214-219
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    • 2011
  • Today, various activities to save energy are being conducted around the world. Even in our country, carbon reduction policy is being conducted for low carbon green growth and with this movement, effort to replace energy sources by recognizing the problems on environment pollution and resource exhaustion due to the indiscrete usage of fossil fuel is being made. Therefore, active study on renewable energy is in progress as part of effort to replace the energy supply through fossil fuel and solar ray industry has rapidly developed receiving big strength of renewable energy policies. The conclusion of this study measuring the surface temperature change of single crystal and polycrystalline PV module in green roof system and non-green roof system aspect are as follows. There was approximately $4^{\circ}C$ difference in PV module temperature in green roof system and non-green roof system aspect and this has the characteristic to decrease 0.5% when the temperature rises by $1^{\circ}C$ when the front side of the module is $20^{\circ}C$ higher than the surrounding air temperature following the characteristic of solar cells. It can be concluded that PV efficiency will be come better when it is $4^{\circ}C$ lower. Also, in result of temperature measurement of the module back side, there was $5^{\circ}C$ difference of PV module installed on the PV module back side and green roof system side on the 5th, $3^{\circ}C$ on the 4th, $2^{\circ}C$ on the 5th to show decreasing temperature difference as the air temperature dropped, but is judged that there will be higher temperature difference due to the evapotranspiration latent heat effect of green roof system floor side as the temperature rises. Based on this data, it is intended to be used as basic reference to maximize efficiency by applying green roof system and PV system when building non-green roof system flat roof.

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Characterization of Microbial Pathogen Bacillus thuringiensis Isolates from Soil Against Mosquito and Silkworm Larvae (II) (토양에서 분리한 살충성 Bacillus thuringiensis의 모기와 누에 유충에 대한 독성효과 (II))

  • Lee, Hyung-Hoan;Yoo, Bo-Rim;Kim, Young-Joo;Won, Nam-Hi;Kim, Hak-Chun
    • Korean Journal of Microbiology
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    • v.31 no.1
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    • pp.17-21
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    • 1993
  • Eight strains of Bacillus thuringiensis were isolated from soil in Korea and characterized. The isolates were named HL-24, HL-25, HL-33, HL-34, HL-35, HL-38, HL-39, HL-40. Strains HL-24 and HL-25 produced irregular parasporal crystals, HL-33 and HL-35 produced bipyramidal crystals, and others were round form in their cells. The biochemical characteristics of the eight isolates were only minor different in specific characteristics to the known serotypes of Bacillus thuringiensis. The HL-25, HL-33 and HL-34 strains showed resistances to cephalothin, colistin and penicillin G, and HL-39 and HL-40 strains were resistant to penicilin G. The strains of HL-24, HL-25, HL-33 and HL-34 were toxic to Bombyx mori lavae and HL-24, HL-25, HL-38, HL-39 and HL-40 strains killed Culex pipiens 3rd instar larvae. The HL-24 and H25 strains showed lethal activity against two kinds of the larvae, however lethality against mosquito larvae was low.

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Dye-sensitized Solar Cells Utilizing Core/Shell Structure Nanoparticle Fabrication and Deposition Process (코어/쉘 구조의 나노입자 제조 및 증착 공정을 활용한 염료감응 태양전지)

  • Jeong, Hongin;Yoo, Jhongryul;Park, Sungho
    • Korean Chemical Engineering Research
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    • v.57 no.1
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    • pp.111-117
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    • 2019
  • This study proposed the fabrication and deposition of high purity crystalline $core-TiO_2/shell-Al_2O_3$ nanoparticles. Morphological properties of $core-TiO_2$ and coated $shell-Al_2O_3$ were confirmed by transmission electron microscope (TEM) and transmission electron microscope - energy dispersive spectroscopy (TEM-EDS). The electrical properties of the prepared $core-TiO_2/shell-Al_2O_3$ nanoparticles were evaluated by applying them to a working electrode of a Dye-Sensitized Solar Cell (DSSC). The particle size, growth rate and the main crystal structure of $core-TiO_2$ were analyzed through dynamic light scattering system (DLS), scanning electron microscope (SEM) and X-ray diffraction (XRD). The $core-TiO_2$, which has a particle size of 17.1 nm, a thin film thickness of $20.1{\mu}m$ and a main crystal structure of anatase, shows higher electrical efficiency than the conventional paste-based dye-sensitized solar cell (DSSC). In addition, the energy conversion efficiency (6.28%) of the dye-sensitized solar cell (DSSC) using the $core-TiO_2/shell-Al_2O_3$ nanoparticles selectively controlled to the working electrode is 26.1% higher than the energy conversion efficiency (4.99%) of the dye-sensitized solar cell (DSSC) using the conventional paste method.

Two Crystal Structures of Dehydrated Ag$^+$ and K$^+$Exchanged Zeolite A, $Ag_{12-x}K_x$-A, x = 1.3 and 2.7

  • Kim, Yang;Song, Seong-Hwan;Park, Jong-Yul;Kim, Un-Sik
    • Bulletin of the Korean Chemical Society
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    • v.9 no.6
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    • pp.338-341
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    • 1988
  • Two crystal structures of fully dehydrated silver and potassium exchanged zeolite A, stoichiometries of $Ag_{9.3}K_{{2.7}^-}A$ (${\alpha}$ = 12.282(2) ${\AA}$) and $Ag_{10.7}K_{{1.3}^-}{\AA}$ (${\alpha}$ = 12.287(2) A) per unit cell, have been determined from 3-dimensional x-ray diffraction data gathered by counter methods. All structures were solved and refined in the cubic space group Pm3m at 21(1)$^{\circ}C$ . The crystals of $Ag_{9.3}K_{{2.7}^-}A$ and $Ag_{10.7}K_{{1.3}^-}A$ were prepared by flow method using exchange solutions in which mole ratios of $AgNO_3$ and $KNO_3$ were 1:10 and 1:5, respectively, with total concentration of 0.05M. The structures of the dehydrated $Ag_{9.3}K_{{2.7}^-}A$ and $Ag_{10.7}K_{{1.3}^-}A$ were refined to yield the final error indices $R_1$ = 0.037 and $R_2$ = 0.040 with 321 reflections, and $R_1$ = 0.042 and $R_2$ = 0.043 with 371 reflections, repectively, for which I > 3${\sigma}$(I). In both structures, eight $Ag^+$ ions are found nearly at 6-ring centers and each $Ag^+$ ion is nearly in the (1 1 1) plane at its O(3) ligands. The 8-ring sites are preferentially occupied by $K^+$ ions in both structures. 1.3 and 1.7 reduced silver atoms per unit cell were found inside of sodalite units of $Ag_{9.3}K_{{2.7}^-}A$ and that of $Ag_{10.7}K_{{1.3}^-}A$, respectively. These reduced silver species were presumably formed from the reduction of $Ag^+$ ions by oxide ions of residual water molecule or of the zeolite framework. These two crystals may be presented as hexasilver cluster in 21.7% and 28.3% of sodalite unit cells for $Ag_{9.3}K_{{2.7}^-}A$ and $Ag_{10.7}K_{{1.3}^-}A$, repectively.

Iron chelating agent, deferoxamine, induced apoptosis in Saos-2 osteosarcoma cancer cells (Saos-2 골육종 세포에서 iron chelating agent, deferoxamine에 의한 apoptosis 유도)

  • Park, Eun Hye;Lee, Hyo Jung;Lee, Soo Yeon;Kim, Sun Young;Yi, Ho Keun;Lee, Dae Yeol;Hwang, Pyoung Han
    • Clinical and Experimental Pediatrics
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    • v.52 no.2
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    • pp.213-219
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    • 2009
  • Purpose:Iron is a critical nutritional element that is essential for a variety of important biological processes, including cell growth and differentiation, electron transfer reactions, and oxygen transport, activation, and detoxification. Iron is also required for neoplastic cell growth due to its catalytic effects on the formation of hydroxyl radicals, suppression of host defense cell activities, and promotion of cancer cell multiplication. Chronic transfusion-dependent patients receiving chemotherapy may have iron overload, which requires iron-chelating therapy. We performed this study to demonstrate whether the iron chelating agent deferoxamine induces apoptosis in Saos-2 osteosarcoma cells, and to investigate the underlying apoptotic mechanism. Methods:To analyze the apoptotic effects of an iron chelator, cultured Saos-2 cells were treated with deferoxamine. We analyzed cell survival by trypan blue and crystal violet analysis, apoptosis by nuclear condensation, DNA fragmentation, and cell cycle analysis, and the expression of apoptotic related proteins by Western immunoblot analysis. Results:Deferoxamine inhibited the growth of Saos-2 cell in a time- and dose-dependent manner. The major mechanism for growth inhibition with the deferoxamine treatment was by the induction of apoptosis, which was supported by nuclear staining, DNA fragmentation analysis, and flow cytometric analysis. Furthermore, bcl-2 expression decreased, while bax, caspase-3, caspase-9, and PARP expression increased in Saos-2 cells treated with deferoxamine. Conclusion:These results demonstrated that the iron chelating agent deferoxamine induced growth inhibition and mitochondrial-dependent apoptosis in osteosarcoma Saos-2 cells, suggesting that iron chelating agents used in controlling neoplastic cell fate can be potentially developed as an adjuvant agent enhancing the anti-tumor effect for the treatment of osteosarcoma.

Kinetic and Structural Characterization for Cofactor Preference of Succinic Semialdehyde Dehydrogenase from Streptococcus pyogenes

  • Jang, Eun Hyuk;Park, Seong Ah;Chi, Young Min;Lee, Ki Seog
    • Molecules and Cells
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    • v.37 no.10
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    • pp.719-726
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    • 2014
  • The ${\gamma}$-Aminobutyric acid (GABA) that is found in prokaryotic and eukaryotic organisms has been used in various ways as a signaling molecule or a significant component generating metabolic energy under conditions of nutrient limitation or stress, through GABA catabolism. Succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde to succinic acid in the final step of GABA catabolism. Here, we report the catalytic properties and two crystal structures of SSADH from Streptococcus pyogenes (SpSSADH) regarding its cofactor preference. Kinetic analysis showed that SpSSADH prefers $NADP^+$ over $NAD^+$ as a hydride acceptor. Moreover, the structures of SpSSADH were determined in an apo-form and in a binary complex with $NADP^+$ at $1.6{\AA}$ and $2.1{\AA}$ resolutions, respectively. Both structures of SpSSADH showed dimeric conformation, containing a single cysteine residue in the catalytic loop of each subunit. Further structural analysis and sequence comparison of SpSSADH with other SSADHs revealed that Ser158 and Tyr188 in SpSSADH participate in the stabilization of the 2'-phosphate group of adenine-side ribose in $NADP^+$. Our results provide structural insights into the cofactor preference of SpSSADH as the gram-positive bacterial SSADH.

Structural and Biochemical Studies Reveal a Putative FtsZ Recognition Site on the Z-ring Stabilizer ZapD

  • Choi, Hwajung;Min, Kyungjin;Mikami, Bunzo;Yoon, Hye-Jin;Lee, Hyung Ho
    • Molecules and Cells
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    • v.39 no.11
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    • pp.814-820
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    • 2016
  • FtsZ, a tubulin homologue, is an essential protein of the Z-ring assembly in bacterial cell division. It consists of two domains, the N-terminal and C-terminal core domains, and has a conserved C-terminal tail region. Lateral interactions between FtsZ protofilaments and several Z-ring associated proteins (Zaps) are necessary for modulating Z-ring formation. ZapD, one of the positive regulators of Z-ring assembly, directly binds to the C-terminal tail of FtsZ and promotes stable Z-ring formation during cytokinesis. To gain structural and functional insights into how ZapD interacts with the C-terminal tail of FtsZ, we solved two crystal structures of ZapD proteins from Salmonella typhimurium (StZapD) and Escherichia coli (EcZapD) at a 2.6 and $3.1{\AA}$ resolution, respectively. Several conserved residues are clustered on the concave sides of the StZapD and EcZapD dimers, the suggested FtsZ binding site. Modeled structures of EcZapD-EcFtsZ and subsequent binding studies using bio-layer interferometry also identified the EcFtsZ binding site on EcZapD. The structural insights and the results of bio-layer interferometry assays suggest that the two FtsZ binding sites of ZapD dimer might be responsible for the binding of ZapD dimer to two protofilaments to hold them together.

Core Circuit Technologies for PN-Diode-Cell PRAM

  • Kang, Hee-Bok;Hong, Suk-Kyoung;Hong, Sung-Joo;Sung, Man-Young;Choi, Bok-Gil;Chung, Jin-Yong
    • JSTS:Journal of Semiconductor Technology and Science
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    • v.8 no.2
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    • pp.128-133
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    • 2008
  • Phase-change random access memory (PRAM) chip cell phase of amorphous state is rapidly changed to crystal state above 160 Celsius degree within several seconds during Infrared (IR) reflow. Thus, on-board programming method is considered for PRAM chip programming. We demonstrated the functional 512Mb PRAM with 90nm technology using several novel core circuits, such as metal-2 line based global row decoding scheme, PN-diode cells based BL discharge (BLDIS) scheme, and PMOS switch based column decoding scheme. The reverse-state standby current of each PRAM cell is near 10 pA range. The total leak current of 512Mb PRAM chip in standby mode on discharging state can be more than 5 mA. Thus in the proposed BLDIS control, all bitlines (BLs) are in floating state in standby mode, then in active mode, the activated BLs are discharged to low level in the early timing of the active period by the short pulse BLDIS control timing operation. In the conventional sense amplifier, the simultaneous switching activation timing operation invokes the large coupling noise between the VSAREF node and the inner amplification nodes of the sense amplifiers. The coupling noise at VSAREF degrades the sensing voltage margin of the conventional sense amplifier. The merit of the proposed sense amplifier is almost removing the coupling noise at VSAREF from sharing with other sense amplifiers.

The effect of 4-hexylresorcinol on xenograft degradation in a rat calvarial defect model

  • Kang, Yei-Jin;Noh, Ji-Eun;Lee, Myung-Jin;Chae, Weon-Sik;Lee, Si Young;Kim, Seong-Gon
    • Maxillofacial Plastic and Reconstructive Surgery
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    • v.38
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    • pp.29.1-29.9
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    • 2016
  • Background: The objective of this study was to evaluate xenograft degradation velocity when treated with 4-hexylresorcinol (4HR). Methods: The scapula of a cow was purchased from a local grocery, and discs (diameter 8 mm, thickness 1 mm) were prepared by trephine bur. Discs treated with 4HR were used as the experimental group. Untreated discs were used as the control. X-ray diffraction (XRD), Fourier transform infrared spectroscopy (FT-IR), antibacterial test, endotoxin test, and scanning electron microscopy (SEM) were performed on the discs. In vivo degradation was evaluated by the rat calvarial defect model. Results: The XRD and FT-IR results demonstrated successful incorporation of 4HR into the bovine bone. The experimental disc showed antibacterial properties. The endotoxin test yielded results below the level of endotoxin contamination. In the SEM exam, the surface of the experimental group showed needle-shaped crystal and spreading of RAW264.7 cells. In the animal experiments, the amount of residual graft was significantly smaller in the experimental group compared to the control group (P = 0.003). Conclusions: In this study, 4HR was successfully incorporated into bovine bone, and 4HR-incorporated bovine bone had antibacterial properties. In vivo experiments demonstrated that 4HR-incorporated bovine bone showed more rapid degradation than untreated bovine bone.

Crystallization and X-Ray Crystallographic Studies of Wild-Type and Mutant Tryptophan Synthase α-Subunits from Escherichia coli

  • Jeong, Mi Suk;Jang, Se Bok
    • Molecules and Cells
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    • v.19 no.2
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    • pp.219-222
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    • 2005
  • The a-subunit of Escherichia coli tryptophan synthase (${\alpha}TS$), a component of the tryptophan synthase ${\alpha}_2{\beta}_2$ complex, is a monomeric 268-residues protein (Mr = 28,600). ${\alpha}TS$ by itself catalyzes the cleavage of indole-3-glycerol phosphate to glyceraldehyde-3-phosphate and indole, which is converted to tryptophan in tryptophan biosynthesis. Wild-type and P28L/Y173F double mutant ${\alpha}$-subunits were overexpressed in E. coli and crystallized at 298 K by the hanging-drop vapor-diffusion method. X-ray diffraction data were collected to $2.5{\AA}$ resolution from the wild-type crystals and to $1.8{\AA}$ from the crystals of the double mutant, since the latter produced better quality diffraction data. The wild-type crystals belonged to the monoclinic space group C2 ($a=155.64{\AA}$, $b=44.54{\AA}$, $c=71.53{\AA}$ and ${\beta}=96.39^{\circ}$) and the P28L/Y173F crystals to the monoclinic space group $P2_1$ ($a=71.09{\AA}$, b=52.70, $c=71.52{\AA}$ and ${\beta}=91.49^{\circ}$). The asymmetric unit of both structures contained two molecules of ${\alpha}TS$. Crystal volume per protein mass ($V_m$) and solvent content were $2.15{\AA}^3\;Da^{-1}$ and 42.95% for the wild-type and $2.34{\AA}^3\;Da^{-1}$ and 47.52% for the double mutant.