• Title/Summary/Keyword: $\alpha$-spectroscopy

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Study on the Copper-Arsenic Green Pigments used on Shamanic Paintings in the 19~20th century (19~20세기 무신도 등에 사용된 구리-비소 녹색 안료에 대한 연구)

  • Oh, Joon Suk;Choi, Jung Eun;Choi, Yoon Hee
    • Journal of Conservation Science
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    • v.31 no.3
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    • pp.193-214
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    • 2015
  • The green pigments of shamanic paintings (83 items) in the 19~20th century were analyzed with X-ray fluorescent spectrometer(XRF), scanning electron microscopy (SEM) and fourier transform infrared spectroscopy (ATR-FTIR). In 60 items, copper and arsenic were detected in green pigments of the paintings by XRF spectra. Cu $K{\alpha}$/As $K{\beta}$ (peak intensity ratio of copper and arsenic) of shamanic paintings of Bokgaedang (shrine), solemn paintings (romance of three kingdoms) of Donggwanwangmyo and unknown enshrined place were 5.93~12.04 and higher compared to 5.67-6.26 of standard emerald greens and 4.01~7.89 of remaining shamanic paintings. The SEM images of crystal forms of copper-arsenic green pigments were various. Crystal forms were divided into oval and round spherulite with intersecting plate crystals and spherulite with agglomerate plate crystals. The crystals of the latter were found in shamanic paintings of Bokgaedang (shrine), solemn paintings (romance of three kingdoms) of Donggwanwangmyo and unknown enshrined place and the former were found in the rest of shamanic paintings. Copper-arsenic green pigments of shamanic paintings were identified as Scheele's green from shamanic paintings of Bokgaedang (shrine) and romance of three kingdoms. Emerald green from the rest of shamanic paintings by ATR-FTIR. From analytical results, it is confirmed that Scheele's green of shamanic paintings of Bokgaedang and romance of three kingdoms was used in the 1850s~1870s and emerald green had been widely used from late 19th century to 1970 in the rest of shamanic paintings.

Bacillus thuringiensis Cry4A and Cry4B Mosquito-larvicidal Proteins: Homology-based 3D Model and Implications for Toxin Activity

  • Angsuthanasombat, Chanan;Uawithya, Panapat;Leetachewa, Somphob;Pornwiroon, Walairat;Ounjai, Puey;Kerdcharoen, Teerakiat;Katzenmeier, Gerd;Panyim, Sakol
    • BMB Reports
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    • v.37 no.3
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    • pp.304-313
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    • 2004
  • Three-dimensional (3D) models for the 65-kDa activated Cry4A and Cry4B $\delta$-endotoxins from Bacillus thuringiensis subsp. israelensis that are specifically toxic to mosquito-larvae were constructed by homology modeling, based on atomic coordinates of the Cry1Aa and Cry3Aa crystal structures. They were structurally similar to the known structures, both derived 3D models displayed a three-domain organization: the N-terminal domain (I) is a seven-helix bundle, while the middle and C-terminal domains are primarily comprise of anti-parallel $\beta$-sheets. Circular dichroism spectroscopy confirmed the secondary structural contents of the two homology-based Cry4 structures. A structural analysis of both Cry4 models revealed the following: (a) Residues Arg-235 and Arg-203 are located in the interhelical 5/6 loop within the domain I of Cry4A and Cry4B, respectively. Both are solvent exposed. This suggests that they are susceptible to tryptic cleavage. (b) The unique disulphide bond, together with a proline-rich region within the long loop connecting ${\alpha}4$ and ${\alpha}5$ of Cry4A, were identified. This implies their functional significance for membrane insertion. (c) Significant structural differences between both models were found within domain II that may reflect their different activity spectra. Structural insights from this molecular modeling study would therefore increase our understanding of the mechanic aspects of these two closely related mosquito-larvicidal proteins.

Time-dependent proteomic and genomic alterations in Toll-like receptor-4-activated human chondrocytes: increased expression of lamin A/C and annexins

  • Ha, Seung Hee;Kim, Hyoung Kyu;Nguyen, Thi Tuyet Anh;Kim, Nari;Ko, Kyung Soo;Rhee, Byoung Doo;Han, Jin
    • The Korean Journal of Physiology and Pharmacology
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    • v.21 no.5
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    • pp.531-546
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    • 2017
  • Activation of Toll-like receptor-4 (TLR-4) in articular chondrocytes increases the catabolic compartment and leads to matrix degradation during the development of osteoarthritis. In this study, we determined the proteomic and genomic alterations in human chondrocytes during lipopolysaccharide (LPS)-induced inflammation to elucidate the underlying mechanisms and consequences of TLR-4 activation. Human chondrocytes were cultured with LPS for 12, 24, and 36 h to induce TLR-4 activation. The TLR-4-induced inflammatory response was confirmed by real-time PCR analysis of increased interleukin-1 beta ($IL-1{\beta}$), interleukin-6 (IL-6), and tumor necrosis factor alpha ($TNF-{\alpha}$) expression levels. In TLR-4-activated chondrocytes, proteomic changes were determined by two-dimensional electrophoresis and matrix-assisted laser desorption/ionization-mass spectroscopy analysis, and genomic changes were determined by microarray and gene ontology analyses. Proteomics analysis identified 26 proteins with significantly altered expression levels; these proteins were related to the cytoskeleton and oxidative stress responses. Gene ontology analysis indicated that LPS treatment altered specific functional pathways including 'chemotaxis', 'hematopoietic organ development', 'positive regulation of cell proliferation', and 'regulation of cytokine biosynthetic process'. Nine of the 26 identified proteins displayed the same increased expression patterns in both proteomics and genomics analyses. Western blot analysis confirmed the LPS-induced increases in expression levels of lamin A/C and annexins 4/5/6. In conclusion, this study identified the time-dependent genomic, proteomic, and functional pathway alterations that occur in chondrocytes during LPS-induced TLR-4 activation. These results provide valuable new insights into the underlying mechanisms that control the development and progression of osteoarthritis.

Biochemical Analysis of Interaction between Kringle Domains of Plasminogen and Prion Proteins with Q167R Mutation

  • Lee, Jeongmin;Lee, Byoung Woo;Kang, Hae-Eun;Choe, Kevine K.;Kwon, Moosik;Ryou, Chongsuk
    • Journal of Microbiology and Biotechnology
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    • v.27 no.5
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    • pp.1023-1031
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    • 2017
  • The conformational change of cellular prion protein ($PrP^C$) to its misfolded counterpart, termed $PrP^{Sc}$, is mediated by a hypothesized cellular cofactor. This cofactor is believed to interact directly with certain amino acid residues of $PrP^C$. When these are mutated into cationic amino acid residues, $PrP^{Sc}$ formation and prion replication halt in a dominant negative (DN) manner, presumably due to strong binding of the cofactor to mutated $PrP^C$, designated as DN PrP mutants. Previous studies demonstrated that plasminogen and its kringle domains bind to PrP and accelerate $PrP^{Sc}$ generation. In this study, in vitro binding analysis of kringle domains of plasminogen to Q167R DN mutant PrP (PrPQ167R) was performed in parallel with the wild type (WT) and Q218K DN mutant PrP (PrPQ218K). The binding affinity of PrPQ167R was higher than that of WT PrP, but lower than that of PrPQ218K. Scatchard analysis further indicated that, like PrPQ218K and WT PrP, PrPQ167R interaction with plasminogen occurred at multiple sites, suggesting cooperativity in this interaction. Competitive binding analysis using $\small{L}$-lysine or $\small{L}$-arginine confirmed the increase of the specificity and binding affinity of the interaction as PrP acquired DN mutations. Circular dichroism spectroscopy demonstrated that the recombinant PrPs used in this study retained the ${\alpha}$-helix-rich structure. The ${\alpha}$-helix unfolding study revealed similar conformational stability for WT and DN-mutated PrPs. This study provides an additional piece of biochemical evidence concerning the interaction of plasminogen with DN mutant PrPs.

Optimization of a Crystallization Process by Response Surface Methodology (반응표면분석법을 이용한 결정화 공정의 최적화)

  • Lee, Se-Eun;Kim, Jae-Kyeong;Han, Sang-Keun;Chae, Joo-Seung;Lee, Keun-Duk;Koo, Kee-Kahb
    • Applied Chemistry for Engineering
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    • v.26 no.6
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    • pp.730-736
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    • 2015
  • Cyclotrimethylene trinitramine (RDX) is a high explosive commonly used for military applications. Submicronization of RDX particles has been a critical issue in order to alleviate the unintended and accidental stimuli toward safer and more powerful performances. The purpose of this study is to optimize experimental variables for drowning-out crystallization applied to produce submicron RDX particles. Effects of RDX concentration, anti-solvent temperature and anti-solvent mass were analyzed by the central composite rotatable design. The adjusted determination coefficient of regression model was calculated to be 0.9984 having the p-value less than 0.01. Response surface plots based on the central composite rotatable design determined the optimum conditions such as RDX concentration of 3 wt%, anti-solvent temperature of $0.2^{\circ}C$ and anti-solvent mass of 266 g. The optimum and experimental diameters of RDX particles were measured to be $0.53{\mu}m$ and $0.53{\mu}m$, respectively. The regression model satisfactorily predicts the average diameter of RDX particles prepared by drowning-out crystallization. Structure of RDX crystals was found to be ${\alpha}$-form by X-ray diffraction analysis and FT-IR spectroscopy.

Antifreeze Activity of Dimerized Type I Antifreeze Protein Fragments (Type I 결빙방지 단백질 조각 이량체의 결빙방지 활성)

  • Kim, Hak Jun
    • Journal of Life Science
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    • v.27 no.5
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    • pp.584-590
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    • 2017
  • Antifreeze proteins (AFPs) bind to ice crystals and inhibit their growth. AFPs are essential for the survival of organisms living in subzero environments. Type I AFP (AFP37) isolated from winter flounder is an ${\alpha}$-helical peptide of 37 residues long. In this study, we attempted to develop short AFP fragments with higher activity and solubility. We designed and synthesized N-terminal 15 and 21 residue-long AFPs, designated AFP15 and 21. Also dimerized AFP15 and 21, designated dAFP15N and dAFP21N, respectively, were generated through disulfide bonds between peptides containing CGG residues added to the N-terminus of AFP15 and AFP21 (designated AFP15N and 21N). Their helical contents and antifreeze activities were assessed using circular dichroism (CD) spectroscopy and a nanoliter osmometer, respectively. The helical content of AFP15 AFP21, AFP15N, AFP21N, dAFP15N and dAFP21N was 47, 48, 23.8, 28, 49.1, and 52%, respectively compared to that of wild type AFP37; the antifreeze activity was 8.4, 9.3, 0.05, 5.6, 12.1, 11.2% respectively, compared to that of wild type AFP37. Contrary to our anticipation, the dimerized peptides showed almost the same antifreeze activity as their monomeric counterparts. These results indicate that the dimerized peptides behave as monomeric peptides due to the high rotational freedom of disulfide bonds connecting two monomeric peptides. The star-shaped ice crystals generated by the peptides also demonstrated weak interaction between ice and peptides.

Preparation of Cobalt-Substituted Iron Oxide Powder from Organometallic Precursors (Ⅱ) (유기금속 전구체로부터 코발트 치환 산화철 분말 제조 (Ⅱ))

  • Kim, Jeong Su;Gang, Han Cheol;Hong, Yang Gi
    • Journal of the Korean Chemical Society
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    • v.38 no.2
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    • pp.92-100
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    • 1994
  • Ultrafine cobalt-substituted iron oxide particles were prepared by the thermal decomposition and oxidation of the new organometallic precursor, $Co_xFe_{1-x}(N_2H_3COO)_2(N_2H_4)_2$ (x = 0, 0.01, 0.02, 0.03, 0.05, 0.10, 1.00). The organometallic precursors were synthesized by the reaction of Co(II) and Fe(II) ion in a mole ratio of x : 1-x with hydrazinocarboxylic acid, and characterized by quantitative analysis, elemental analysis and infrared spectroscopy. The mechanistic study on the thermal decomposition of the organometallic precursors was performed by TG-DTG and DSC. The cobalt-substituted iron oxide particles were obtained by the heat treatment of the precursors at $350^{\circ}C$ and $450^{\circ}C$ for six hours in air. The prepared iron oxide was found to have two phases such as ${\gamma}-Fe_2O_3$ and a mixture of ${\gamma}-Fe_2O_3\;and\;{\alpha}-Fe_2O_3$ at $350^{\circ}C$ and $450^{\circ}C$ respectively. The particle shape was equiaxial and the particle size was less than 0.05 ${\mu}m.$ The coercivity and squareness of the cobalt substituted iron oxide particles increased with increasing cobalt content. Both coercivity and squareness showed higher values at $450^{\circ}C.$

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Study on the Charge-Transfer Complexes Formed between the Derivatives of Nitrobenzene and Some Organic Solvent Molecules (용매성 유기분자와 니트로벤젠 및 그의 유도체와의 전하전이 착물에 관한 연구)

  • Doo-Soon Shin;Si-Joong Kim
    • Journal of the Korean Chemical Society
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    • v.17 no.2
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    • pp.85-94
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    • 1973
  • The stability constants of the charge-transfer complexes formed between three derivatives of nitrobenzene, i.e., 1,3,5-trinitrobenzene, m-dinitrobenzene, nitrobenzene and eleven organic molecules such as $\alpha-picoline$, pyridine, dimethylsulfoxide, N, N'-dimethylacetamide, tetrahydrofurane, 1, 4-dioxane, diethyl ether, acetonitrile, propylene oxide, epichlorohydrine, and methyl acetate, have been determined by ultraviolet absorption spectroscopy in carbon tetrachloride solution at 25.0$^{\circ}C$. The parameters of the electrostatic effect ($E_D$) and covalent effect ($C_D$) for the eleven organic compounds have been calculated from the modified equation of the double-scale enthalpy,$logK = E_AC_A+E_DC_D$ and also the shift of C=O vibrational frequency in infrared spectra for N,N'-dimethylacetamide have been measured from the solutions of above organic compounds. The empirical equation, ${\Delta}{\nu}_{C=O} = 37.4-5.47E_D+12.1C_D$, related to the parameters and the frequency shift has been derived. It seems that the stabilities of the complexes principally depend on the covalent effect. Especially it is found that $\pi$ orbitals in molecules, in addition to the parameters, play the important role in forming the charge-transfer complexes.

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Studies on the carotenoids in the viscera of abalone (Haliotis discus hannai) (전복(Haliotis discus hannai) 내장(內臟)의 Carotenoid에 관(關)한 연구(硏究))

  • Ahn, Seung-Yo
    • Applied Biological Chemistry
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    • v.17 no.4
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    • pp.257-274
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    • 1974
  • The studies on the carotenoids in the viscera of abalone (Haliotis discus hannai) have been-carried out. The pigments were extracted with acetone-methanol mixture (4 : 1) from the viscera of abalones which were caught around the coastal water of Korea from March to August. The individual carotenoid in the extracts was separated and purified by the silica gel TLC, $Mg(OH)_2$ impregnated paper chromatography and $Mg_2(OH)_2CO_3$ TLC. The isolated eleven carotenoids were investigated and identified by epoxide test, partition test, reduction with sodium borohydride, alkaline hydrolysis, co-chromatography and comparative test with reference carotenoids and electronic and IR absorption spectrophotometry. ${\alpha}$-Carotene, ${\beta}$-carotene. lutein, zeaxanthin, siponaxanthin, siponein, fucoxanthin, loroxan-thin-like and fucoxanthinol-like have been identified among the eleven carotenoids isolated. It has been found that fucoxanthin, on alkaline treatment, was transformed to the product of which chromophore was the same one as fucochrome and semifucoxanthol. Among the identified nein carotenoids siphonaxanthin, siponein, fucoxanthin, loroxanthin-like and fucoxanthinol-like have not been reported previously to be contained in the shellfish.

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Self-Assembly of Vanadium Borophosphate Cluster Anions: Synthesis and Structures of (NH4)(C2H10N2)5.5[Cu(C2H8N2)2]3[V2P2BO12]6·17H2O and (NH4)(C2H10N2)3.5[Cu(C2H8N2)2]5[V2P2BO12]6·18H2O

  • Jung, Kyung-Na;Cho, Yoon-Suk;Yun, Ho-Seop;Do, Jung-Hwan
    • Bulletin of the Korean Chemical Society
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    • v.26 no.8
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    • pp.1185-1189
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    • 2005
  • Two new copper vanadium borophosphate compounds, $(NH_4)(C_2H_{10}N_2)_{5.5}[Cu(C_2H_8N_2)_2]_3[V_2P_2BO_{12}]_6{\cdot}17H_2O,\;Cu-VBPO1\;and\;(NH_4)(C_2H_{10}N_2)_{3.5}[Cu(C_2H_8N_2)_2]_5[V_2P_2BO_{12}]_6{\cdot}18H_2O$, Cu-VBPO2 have been hydrothermally synthesized and characterized by single crystal X-ray diffraction, thermogravimetric analysis, IR spectroscopy, and elemental analysis. The structure of Cu-VBPO1 contains a layer anion, {$[Cu(C_2H_8N_2)_2]_3[V_2P_2BO_{12}]_6$}$^{12-}$, whereas Cu-VBPO2 has an open framework anion, {$[Cu(C_2H_8N_2)_2]_5[V_2P_2BO_{12}]_6$}$^{8-}$. Crystal Data: $(NH_4)(C_2H_{10}N_2)_{5.5}[Cu(C_2H_8N_2)_2]_3[V_2P_2BO_{12}]_6{\cdot}17H_2O$, monoclinic, space group I2/m (no. 12), $\alpha$ = 15.809(1) $\AA$, b = 31.107(2) $\AA$, c = 12.9343(8) $\AA$, $\beta$ = 104.325(1)$^{\circ}$, Z = 2; $(NH_4)(C_2H_{10}N_2)_{3.5}[Cu(C_2H_8N_2)_2]_5[V_2P_2BO_{12}]_6{\cdot}18H_2O$, tetragonal, space group $P4_2$/mnm (no.136), $\alpha$ = 26.832(1) $\AA$, c = 18.021(1) $\AA$, Z = 4.