• Archives of Pharmacal Research
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• v.29 no.1
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• pp.50-58
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• 2006

Translationally controlled tumor protein (TCTP), also known as histamine releasing factor (HRF), is found abundantly in different eukaryotic cell types. The sequence homology of TCTP between different species is very high, belonging to the MSS4/DSS4 superfamily of proteins. TCTP is involved in both cell growth and human late allergy reaction, as well as having a calcium binding property; however, its primary biological functions remain to be clearly elucidated. In regard to many possible functions, the TCTP of Plasmodium falciparum (Pf) is known to bind with an antimalarial agent, artemisinin, which is activated by heme. It is assumed that the endoperoxide-bridge of artemisinin is opened up by heme to form a free radical, which then eventually alkylates, probably to the Cys14 of PfTCTP. Study of the docking of artemisinin with heme, and subsequently with PfTCTP, was carried out to verify the above hypothesis on the basis of structural interactions. The three dimensional (3D) structure of PfTCTP was built by homology modeling, using the NMR structure of the TCTP of Schizosaccharomyces pombe as a template. The quality of the model was examined based on its secondary structure and biological function, as well as with the use of structure evaluating programs. The interactions between artemisinin, heme and PfTCTP were then studied using the docking program, FlexiDock. The center of the peroxide bond of artemisinin and the Fe of heme were docked within a short distance of $2.6{\AA}$, implying the strong possibility of an interaction between the two molecules, as proposed. When the activated form of artemisinin was docked on the PfTCTP, the C4-radical of the drug faced towards the sulfur of Cys14 within a distance of $2.48{\AA}$, again suggesting the possibility of alkylation having occurred. These results confirm the proposed mechanism of the antimalarial effect of artemisinin, which will provide a reliable method for establishing the mechanism of its biological activity using a molecular modeling study.

• Journal of the Korean Electrochemical Society
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• v.9 no.4
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• pp.158-169
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• 2006

The present article is concerned with the overview of the chemically/surface modified cubic spinel $LiMn_2O_4$ as a cathode electrode far lithium ion secondary batteries. Firstly, this article presented a comprehensive survey of the cubic spinel structure and its correlated electrochemical behaviour of $LiMn_2O_4$. Subsequently, the various kinds of the chemically/surface modified $LiMn_2O_4$ and their electrochemical characteristics were discussed in detail. Finally, this article reviewed our recent research works published on the mechanism of lithium transport through the chemically/surface modified $Li_{1-\delta}Mn_2O_4$ electrode from the kinetic view point by the analyses of the experimental potentiostatic current transients and ac-impedance spectra.

• Journal of Photoscience
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• v.3 no.2
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• pp.71-76
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• 1996

Anil K. Singh, Mrunalini M. Kapil, Department of Chemistry, Indian Institute of Technology Bombay - 400076, INDIA Purple membrane (PM, $\lambda$$_{max}$ 570 nm) of H. halobium on treatment with sulphuric acid changes its colour to blue ($\lambda$$_{max}$ 608 nm). The purple chromophore can be regenerated from the blue chromophore by exogeneous addition of anions such as CI$^-$ and HPO$_4^{2-}$. Chloride ion is found to be more effective than the dibasic phosphate ion in regenerating the purple chromophore. Nevertheless, one thing common to the anion regeneration is that both CI$^-$ and HPO$_4^{2-}$ show marked pH effect. At pH 1.0 the efficiency of regeneration of the purple chromophore is greater than at pH 2.0, for the same anion concentration. Fluorescence and circular dichroic studies indicate that the proteins do not undergo drastic changes at the secondary' or tertiary structure level and the native structure is preserved during this transition. However, chromophoric-site interactions between retinal and the apoprotein are affected during this colour transition. A molecular mechanism is advanced for this transition.

• BMB Reports
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• v.31 no.6
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• pp.536-541
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• 1998

The cDNA clone encoding the antibacterial peptide (SL-1) was isolated from the fat body of the common cutworm, Spodoptera litura, immunized with E. coli K12. The primary structure analysis revealed that its deduced amino acid sequence showed the characteristics of the cecropin family antibacterial peptides and that the amino acid residues highly conserved in the antibacterial peptides from moths and flies were also conserved, implying that SL-1 was a cecropin-like, and especially cecropin B-like, peptide. The predicted secondary structure of the mature SL-1 consists of three domains: (i) an amphiphilic ${\alpha}$-helical domain (Ile-4 to Gly-18); (ii) the hinge region (Gly-23 and Pro-24); and (iii) a hydrophobic domain (Ala-25 to IIe-38).

• BMB Reports
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• v.40 no.5
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• pp.740-748
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• 2007

To gain insight into the structure and function of repressor proteins of bacteriophages of gram-positive bacteria, repressor of temperate Staphylococcus aureus phage ${\phi}11$ was undertaken as a model system here and purified as an N-terminal histidine-tagged variant (His-CI) by affinity chromatography. A ~19 kDa protein copurified with intact His-CI (~ 30 kDa) at low level was resulted most possibly due to partial cleavage at its Ala-Gly site. At ~10 nM and higher concentrations, His-CI forms significant amount of dimers in solution. There are two repressor binding sites in ${\phi}11$ cI-cro intergenic region and binding to two sites occurs possibly by a cooperative manner. Two sites dissected by HincII digestion were designated operators $O_L$ and $O_R$, respectively. Equilibrium binding studies indicate that His-CI binds to $O_R$ with a little more strongly than $O_L$ and binding species is probably dimeric in nature. Interestingly His-CI binding affinity reduces drastically at elevated temperatures ($32-42^{\circ}C$). Both $O_L$ and $O_R$ harbor a nearly identical inverted repeat and studies show that ${\phi}11$ repressor binds to each repeat efficiently. Additional analyses indicate that ${\phi}11$ repressor, like $\lambda$ repressor, harbors an N-terminal domain and a C-terminal domain which are separated by a hinge region. Secondary structure of ${\phi}11$ CI even nearly resembles to that of $\lambda$ phage repressor though they differ at sequence level. The putative N-terminal HTH (helix-turn-helix) motif of ${\phi}11$ repressor belongs to the HTH -XRE-family of proteins and shows significant identity to the HTH motifs of some proteins of evolutionary distant organisms but not to HTH motifs of most S. aureus phage repressors.

• Molecules and Cells
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• v.21 no.2
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• pp.229-236
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• 2006

Gaegurin 4 (GGN4), a novel peptide isolated from the skin of a Korean frog, Rana rugosa, has broad spectrum antimicrobial activity. A number of amphipathic peptides closely related to GGN4 undergo a coil to helix transition with concomitant oligomerization in lipid membranes or membrane-mimicking environments. Despite intensive study of their secondary structures, the oligomeric states of the peptides before and after the transition are not well understood. To clarify the structural basis of its antibiotic action, we used analytical ultracentrifugation to define the aggregation state of GGN4 in water, ethyl alcohol, and 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP). The maximum size of GGN4 in 15% HFIP corresponded to a decamer, whereas it was monomeric in buffer. The oligomeric transition is accompanied by a cooperative 9 nm blue-shift of maximum fluorescence emission and a large secondary structure change from an almost random coil to an ${\alpha}$-helical structure. GGN4 induces pores in lipid membranes and, using electrophysiological methods, we estimated the diameter of the pores to be exceed $7.3{\AA}$, which suggests that the minimal oligomer structure responsible is a pentamer.

• Korean Journal of Comparative Education
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• v.26 no.3
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• pp.23-50
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• 2016

The purpose of this study was to explore the status of 'Gesamtschule' (eng. Comprehensive school) in Germany and to suggest future direction for Korean education. To achieve this purpose, this study explored 1)the background of adopting Gesamtschule and its developing process; 2)Change of school structure since 2000 and the status of Gesmatschule. Results of this study indicated that 1)Changing school structure in Germany focused on closing educational gap caused by social class differentials; 2)Gesamtschule and other school model, similar with Gesamtschule are spreading widely in relation to change of school structure in secondary education; 3)Expanding this school model contributed to closing educational gap by analysing of recent results of PISA. This study suggested that efforts for closing educational gab in korean school should not only concentrate on supporting students, but also accompany discussion about change of school structure.

• Bulletin of the Korean Chemical Society
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• v.31 no.12
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• pp.3521-3524
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• 2010

MTH1880 is a hypothetical protein derived from Methanobacterium thermoautotrophicum, thermophilic methanogen. The solution structure determined by NMR spectroscopy showed that it has a novel $\alpha+\beta$-fold with a highly acidic ligand binding pocket. Since MTH1880 maintains its ultra-stable structural characteristics at both high temperature and pressure, it has been considered as an excellent model for studying protein folding. To initiate the structural and folding study of MTH1880 in proving its unusual stability, we performed the site directed mutagenesis and biochemical analysis of MTH1880 mutants. Data from circular dichroism and NMR spectroscopy suggest that the point mutations perturbed the structural stability of protein even though the secondary structure is retained. This study will provide the useful information in understanding the role of participating residues during folding-unfolding process and our result will be used in designing further folding experiments for hyper-thermopile proteins like MTH1880.

• Journal of the Korean Magnetic Resonance Society
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• v.13 no.1
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• pp.56-63
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• 2009

SWIRM domain, a core domain of SRG3 is well conserved in SW13, RSC8, and MOIRA family proteins. To understand structural basis for cellular functions of the SWIRM domain, we have initiated biochemical and structural studies on SWIRM domain and mutants using gelfiltration chromatography, circular dichroism and NMR spectroscopy. The structural properties of the mutant SWIRM domains (K34A and M75A) have been characterized, showing that the structures of both wild-type and mutant proteins are a-helical conformation. The data conclude that mutations at interaction sites of its binding partner protein do not affect its secondary and tertiary structure.

• Advances in materials Research
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• v.7 no.2
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• pp.105-118
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• 2018

Magnesium and its alloys are attracted towards all engineering applications like automotive, marine, aerospace etc. due to its inherent high strength to weight ratio. But, extensive use of Mg alloys is limited to the current scenario because of low wear and corrosion resistance behavior. However, equal channel angular press is one of the severe plastic deformation technique which has been effective method to improve the wear and corrosion resistance by achieving fine grain structure. In this study, the effect of grain refinement on wear and corrosion resistance of AZ80 Mg alloys were investigated. The wear behavior of the coarse and fine-grained Mg alloys was examined through $L_9$ orthogonal array experiments in order to comprehend the wear behavior under varies control parameters. It was shown that ECAPed alloy increased the wear and corrosion resistance of the Mg alloy through the formation of fine grain and uniform distribution of secondary ${\beta}-phase$. Also, the performance of AZ80 Mg alloy for these changeswas discussed through SEM morphology.