• Title/Summary/Keyword: dimer formation

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Biochemical and Structural Analysis of Hormone-sensitive Lipase Homolog EstE7: Insight into the Stabilized Dimerization of HSL-Homolog Proteins

  • Nam, Ki-Hyun;Park, Sung-Ha;Lee, Won-Ho;Hwang, Kwang-Yeon
    • Bulletin of the Korean Chemical Society
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    • v.31 no.9
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    • pp.2627-2632
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    • 2010
  • Hormone sensitive lipase (HSL) plays a major role in energy homeostasis and lipid metabolism. Several crystal structures of HSL-homolog proteins have been identified, which has led to a better understanding of its molecular function. HSL-homolog proteins exit as both monomer and dimer, but the biochemical and structural basis for such oligomeric states has not been successfully elucidated. Therefore, we determined the crystal structure of HSL-homolog protein EstE7 from a metagenome library at $2.2\;{\AA}$ resolution and characterized the oligomeric states of EstE7 both structurally and biochemically. EstE7 protein prefers the dimeric state in solution, which is supported by its higher enzymatic activity in the dimeric state. In the crystal form, EstE7 protein shows two-types of dimeric interface. Specifically, dimerization via the external ${beta}8$-strand occurred through tight association between two pseudosymmetric folds via salt bridges, hydrogen bonds and van der Waals interactions. This dimer formation was similar to that of other HSL-homolog protein structures such as AFEST, BEFA, and EstE1. We anticipate that our results will provide insight into the oligomeric state of HSL-homolog proteins.

Ab initio DFT studies on dimerization and one-dimensional (1-D) polymerization of M@$Au_{12}$ (M = W, Mo) clusters

  • Park, So-Ra;Kim, Gunn;Kwon, Young-Kyun
    • Proceedings of the Korean Vacuum Society Conference
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    • 2010.08a
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    • pp.271-271
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    • 2010
  • Using ab initio density functional theory, we investigate the dimerization and one-dimensional (1-D) polymerization of metal-encapsulated gold nanoclusters, M@$Au_{12}$ (M=W, Mo) and their structural and electronic properties. M@$Au_{12}$ clusters with a magic number 13 can form icosahedral and cuboctahedral structures. We consider various dimer configurations with different compounds and symmetries to find the most stable dimer structure in each case. Au atoms in the one cluster, which participate directly in dimerization, tend to form triangular bonds together with counterpart Au atoms in the other. It is found that both M@$Au_{12}$ and M@$Au_{12}$ clusters are stabilized by about 3 eV due to dimerization. We also calculate and compare the electronic and magnetic properties of different dimerized clusters. Based on our investigation on dimerization, we further study on 1-D polymerization of M@$Au_{12}$ with different compounds and symmetries. We will also discuss their formation energies as well as their electronic and magnetic properties.

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Expression and characterization of the recombinant human galectin-3 (유전자 재조합 Human galectin-3의 발현과 성상)

  • Kim, Byung-gyu;Woo, Hee-jong
    • Korean Journal of Veterinary Research
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    • v.37 no.3
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    • pp.547-554
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    • 1997
  • Galectin-3 is known as an animal ${\beta}$-galactoside-binding lectin charicterized with S-type carbohydrate recognition domain. It plays a role in growth, adherence and movement of cells. It is, also, related to the cell transformation and metastasis of tumor cells. In this study, we have expressed and purified recombinant human galectin-3 (rHgalectin-3) using E coli system and asialofetuin affinity chromatography for the future development of monoclonal antibody to Hgalectin-3, which is suggested as the tumor marker for the gastric and thyroid gland cancers. Expressed protein was confirmed as the Hgalectin-3 by immunoblot with cross-reactive murine monoclonal antibody. Lectin activity and specificity of purified protein were, also, confirmed by the competitive inhibition with galectin-3 specific carbohydrate, lactose. Like physiological galectin-3, lectin activity of the molecule was not changed in nonreduced condition. Dimer formation, furthermore, was observed at high concentration of the protein even in the reduced condition, which is well known in physiological galectin-3. These results showed purified rHgalectin-3 has the same activity and molecular nature compared to the physiological galectin-3.

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Effect of Protonic Acids on the Reaction Rate in Chemical Polymerization of Polyaniline (폴리아닐린의 화학적 중합 시 반응속도에 미치는 양성자산의 영향)

  • Hong, Jang-Hoo;Jang, Beom Soon
    • Applied Chemistry for Engineering
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    • v.16 no.5
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    • pp.684-688
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    • 2005
  • Aniline was polymerized in various protonic acid (HF, HC1, HBr, HI, $H_2SO_4$) aqueous solutions with different acidity. During the reaction, the dimer formation and the reaction rate were examined as functions of acidity (pH) and the size of counter ions. Open-circuit potential measurements were carried out to investigate the effect of protonic acid on the reaction rate. The results showed that polymerization rate in HF aqueous solution was very slow and polymerization did not occur in HI aqueous solution. These results were explained in terms of acidity and power of oxidation. The ratio of formation of dimers varied with the kind of protonic acid, and the results were explained with the nucleophilicity, solvation effect, and mobility of counter ions.

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.

Spectroscopic Evidence for Aggregation of Stilbene Derivatives in Solution

  • Aguiar, M.;Akcelrud, L.;Pinto, M.R.;Atvars, T.D.Z.;Karasz, F.E.;Saltiel, Jack
    • Journal of Photoscience
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    • v.10 no.1
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    • pp.149-155
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    • 2003
  • The absorption, fluorescence and fluorescence-excitation spectra of concentrated toluene solutions of selected para substituted trans-stilbene derivatives provide strong evidence for aggregation. A red-shifted fluorescence spectrum peaking at 420 nm gains in intensity as the stilbene concentration is increased. The excitation spectrum of this new emission is well to the red of the normal stilbene absorption spectrum, consistent with the appearance of a red shifted shoulder in the UV spectrum. Formation of a fluorescent ground state dimer (or higher aggregate) is proposed to account for these observations. The presence of polar substituents is crucial to the formation of this ground state complex.

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Association of Riboflavin and Drug Molecules (Riboflavin과 약품 분자와의 회합)

  • 유병설
    • YAKHAK HOEJI
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    • v.28 no.2
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    • pp.101-127
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    • 1984
  • The study of interaction between riboflavin derivatives and biologically active substances was reviewed. With combination of spectroscopic methods such as NMR, UV, Fluorescence and IR, informations about interaction mechanism including hydrogen bond formation, conformation of association complex, and association constant were obtained. 1. Riboflavin associated with adenine but not with other bases found in the nucleic acids. -CONHCO- group was included in the formation of hydrogen bond with adenine. 2. Riboflavin interacted with alcohol to make a 1 : 1 association complex through the 3N-imino and 2C-carbonyl group of the isoalloxazine ring and the hydroxyl group of the alcohols. 3. Riboflavin associated with salicylates to produce the cyclic hydrogen-bonded dimer. The strongest complex was formed with salicylic acid, a weaker one with aspirin, and an even weaker one with salicylamide. 4. Other bio-active substances, orotic acid and inhibitors such as phenol, trichloroacetic acid and indol also formed hydrogen bond with riboflavin. 5. Reduced riboflavin showed strong self-association to produce the cyclic hydrogen-bonded complex and it associated with adenine and with cytosine to form 1 : 3 complex.

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Purification and Characterization of an Extracellular Levansucrase from Zymomonas mobilis ZM1(ATCC 10988). (Zymomonas mobilis ZM1이 생산하는 균체외 Levansucrase의 정제 및 특성)

  • 송기방;서정우;주현규;이상기
    • Microbiology and Biotechnology Letters
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    • v.26 no.4
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    • pp.309-315
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    • 1998
  • An extracellular levansucrase, which catalyzes the formation of levan from sucrose, from the culture broth of Zymomonas mobilis ZM1 was purified by conventional column purification methods. The final purification yield was 18.3 fold of the crude enzyme from Z. mobilis, with 16.5 % of the enzyme recovered in the preparation step. The molecular weight of the enzyme was estimated to be 91,000 by Superose 12 gel filtration, and 45,000 by SDS-PAGE, indicating that levansucrase is a dimer. The optimum pH for the enzyme activity was around pH 4.0 for sucrose hydrolysis, and was around pH 5.0 for levan formation. The enzyme was inhibited by some metal ions, such as Hg$\^$2+/ and Cu2$\^$2+/, and 50% of inhibition was observed with 5mM EDTA. The enzyme activity was enhanced by the presence of detergent Triton X-100, but inhibited by SDS completely The enzyme catalyzes the liberation of reducing sugars, oligosacccharides and the formation of fructose polymer(levan). The enzyme also catalyzes the transfructosylation reaction of fructose moiety from sucrose to various sugar acceptor molecules, including sugar alcohols.

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Effect of Organic Residue on the Continuous Pyrolysis of Waste Polystyrene (연속식 폐 EPS 열분해 반응에 대한 잔류물의 영향)

  • Yoon, Byung Tae;Kim, Seong Bo;Lee, Sang Bong;Choi, Myoung Jae
    • Korean Chemical Engineering Research
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    • v.43 no.1
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    • pp.125-128
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    • 2005
  • Oil formation rate, composition of crude oil and formation of side products such as ${\alpha}-methyl$ styrene, ethyl benzene, benzene, toluene, dimer and trimer on thermal degradation of polystyrene were affected by various factors. Especially, formation of organic residue formed during reaction gave an important influence on formation of oil and composition of crude oil. Also, composition of formed crude oil showed a significant difference on reaction time. These results were caused by organic residue and carbonized solid formed during continuous reaction. Increase of residue and carbonized solid gave a decrease of yield of styrene and an increase of formation of ${\alpha}-methyl$ styrene, ethyl benzene, benzene, toluene. New reaction system was proposed for continuous operation at the thermal degradation of polystyrene.

Synthesis of Ochnaflavone and Its Inhibitory Activity on PGE2 Production

  • Kim, Sung Soo;Vo, Van Anh;Park, Haeil
    • Bulletin of the Korean Chemical Society
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    • v.35 no.11
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    • pp.3219-3223
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    • 2014
  • Ochnaflavone, a naturally occurring biflavonoid composed of two units of apigenin (5,7,4'-trihydroxyflavone) joined via a C-O-C linkage, was first synthesized and evaluated its inhibitory activity on $PGE_2$ production. Total synthesis was accomplished through modified Ullmann diaryl ether formation as a key step. Coupling reactions of 4'-halogenoflavones and 3'-hydroxy-5,7,4'-trimethoxyflavone were explored in diverse reaction conditions. The reaction of 4'-fluoro-5,7-dimethoxyflavone (2c) and 3'-hydroxy-5,7,4'-trimethoxyflavone (2d) in N,N-dimethylacetamide gave the coupled compound 3 in 58% yield. Synthetic ochnaflavone strongly inhibited PGE2 production ($IC_{50}=1.08{\mu}M$) from LPS-activated RAW 264.7 cells, which was due to reduced expression of COX-2. On the contrary, the inhibition mechanism of wogonin was somewhat different from that of ochnaflavone although wogonin, a natural occurring anti-inflammatory flavonoid, showed strong inhibitory activity of $PGE_2$ production ($IC_{50}=0.52{\mu}M$), and seems to be COX-2 enzyme inhibition. Our concise total synthesis of ochnaflavone enable us to provide sufficient quantities of material for advanced biological studies as well as to efficiently prepare derivatives for structure-activity relationship study.