• International conference on construction engineering and project management
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• 2015.10a
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• pp.344-348
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• 2015

The image data of the web camera is used to identify the construction status of the site in a remote office and it can be used for safety management. This study develops a construction schedule simulation system based on the active nD object linked with real image data of web camera from the construction site. The progress control method by 4D object uses a method that the progress of each activity is represented with different colors by progress status. Since this method is still based on a virtual reality object, it is less realistic description for practical engineers. Therefore, in order to take advantage of BIM more realistic, the real image of actual construction status and 4D object of planned schedule in a data date should be compared in a screen simultaneously. Those methodologies and developed system are verified in a case project where a web camera is installed for the verification of the system.

• BMB Reports
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• v.33 no.1
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• pp.43-48
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• 2000

4-Aminobutyrate aminotransferase is a key enzyme of the 4-aminobutyric acid shunt. It converts the neurotransmitter 4-aminobutyric acid to succinic semialdehyde. In order to study the structural and functional aspects of catalytically active Cys residues of pig brain 4-aminobutyrate aminotransferase, we purified the active form in E. coli by coproduction of thioredoxin. The structural arrangement for functional requirements of a dimeric protein using a bifunctional sultbydryl reagent was then characterized, and the spatial proximity between the essential SH groups and a cofactor (pyridoxal-5'-phosphate) binding site was determined. The bifunctional sultbydryl reagent DMDS reacted with the enzyme at the ratio of one molecule per enzyme dimer. This resulted in an approximately 50% loss of enzymatic activity. The spatial proximity of the distance between the essential SH groups and the cofactor-binding site was determined by the energy transfer measurement technique. The result (approximate 20 ${\AA}$) suggested that cross-linking of two sulfhydryl groups with DMDS is not near a PLP binding site.

• Journal of Pharmaceutical Investigation
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• v.26 no.3
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• pp.155-168
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• 1996

The active site of cyclooxygenase was modeled by complementary receptor-cavity mapping procedure using 3D structures of the non-steroidal antiinflammatory drugs (NSAIDs). A total of 50 NSAIDs were chosen as data ligands which compete the same site on the enzyme. Partial atomic charges were estimated, and the energetic differences for various conformations were calculated so as to meet the need for a most efficient overlapping of the probably-equivalent functional groups of the ligand molecules. The structure activity relationships of the NSAIDs, if available, were fully considered throughout the modeling. The overall shape of the model obtained is similar to a boot-without-bottom. Most of inner surface of the cavity appeared as hydrophobic; two polar counterparts except the carboxyl-binding position were found. By this model, some clear explanations could be given on the experimental observations which were not satisfiably understood yet.

• BMB Reports
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• v.35 no.2
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• pp.244-247
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• 2002

Replacement of the Asp-84 residue of the deoxyguanosine kinase subunit of the tandem deoxyadenosine kinase/deoxyguanosine kinase (dAK/dGK) from Lactobacillus acidophilus R-26 by Ala, Asn, or Glu produced increased $K_m$ values for deoxyguanosine on dGK. However, it did not seem to affect the binding of Mg-ATP. The Asp-84 dGK replacements bad no apparent effect on the binding of deoxyadenosine by dAK. However, the mutant dGKs were no longer inhibited by dGTP, normally a potent distal end-product inhibitor of dGK. Moreover, the allosteric activation of dAK activity by dGTP or dGuo was lost in the modified heterodimeric dAK/dGK enzyme. Therefore, it seems very likely that Asp-84 participates in dGuo binding at the active site of the dGK subunit of dAK/dGK from Lactobacillus acidophilus R-26.

• Proceedings of the Korean Society for Bioinformatics Conference
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• 2005.09a
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• pp.35-40
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• 2005

Interaction of twelve erythromycin A analogues with 50S ribosomal subunit were studied employing AutoDock 3.0.5. Results showed that all active macrolides bound at the same binding site with erythromycin A in contrast to the inactive analogues which bound at location slightly different than erythromycin A. The binding site showed consistency with the X-ray data from the perspectives of hydrogen bonding and hydrophobic interactions formed by erythromycins, roxithromycin, azithromycin, cethromycin and telithromycin with the ribosome. The inactive derivatives of erythromycin A anhydride showed higher binding free energy, while 5-desosaminyl erythronolides A and B even though having quiet similar values of binding free energy with the active analogues, docked at binding sites which are quiet different than the active analogues. These results suggest the molecular docking technique can be used in predicting the binding of erythromycin A analogues to their ribosomal target.

• Korean Journal of Ecology and Environment
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• v.35 no.4 s.100
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• pp.266-272
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• 2002

For analyzing function of a microbial ecosystem which was created under the artificial vegetation island (AVI) installed at Lake Paldang, zooplankton and bacterial numbers and exoenzyme activities (${\beta}$-glucosidase and phosphatase) were measured biweekly from 3 November 2()()1 to 20 April 2002 at AVI site and control site. Under the AVI, the water quality was worse than control site in term of comparing the environmental parameters. But, zooplankton number of AVI site was 25 times higher than that of control site. Respiratory active bacterial numbers were 3-8 times higher at AVI site. In addition, enzymatic activities were higher at AVI site than those of control site. These results suggest that the zooplankton-phytoplankton-bacteria relationships are closely coupled with each other and organic materials are eliminated by respiration of zooplankton and bacterial activities.

• Science of Emotion and Sensibility
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• v.20 no.2
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• pp.59-72
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• 2017

In the flood of information, many consumers want to choose the style that is suitable for their sensibility, which is usefulness and need for personalized services have been steadily increasing. This study made a video of personalized internet shopping mall and then university students (N=170) who have been using the internet shopping mall were asked to experience this and the change in consumer response was measured. According to level of personalization, this study found difference of web-site evaluation, satisfaction/internet behavior and quality evaluations of products. With regard to preferred types of internet shopping malls and the number of access, the difference was investigated. The results are as follows. First, subjects who experienced internet shopping mall of active personalization showed higher level of active personalization. Level of passive personalization differed depending on preferred types of internet shopping malls, for example, people who prefer online apparel shopping mall were low but people who prefer complex big shopping mall and social commerce were high. Second, after experiencing internet shopping mall of active personalization, satisfaction/internet behavior and quality evaluations of products did not change but passive personalization decreased and active personalization and web-site evaluation increased. Third, the number of access to internet shopping mall positively correlated with satisfaction/internet behavior and web-site evaluation, on the other hand, active personalization negatively correlated with satisfaction/internet behavior and web-site evaluation.

• BMB Reports
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• v.32 no.4
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• pp.358-362
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• 1999

dTDP-D-glucose 4,6-dehydratase as an oxidoreductase catalyzes the conversion of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose, which is essential for the formation of 6-deoxysugars. dTDP-D-glucose 4,6-dehydratase shows remarkable sterochemical convergence in which displacement of the C-6 hydroxyl group by a C-4 hydrogen proceeds intramolecularly with inversion of configuration. The reaction mechanism is known to be oxidation, dehydration, and reduction by bases mediating proton transfer and $NAD^+$ cofactor. In this study, the bases in the active site domain are proposed to be His-79 and His-300 from a comparison of the peptides of the dehydratase and UDP-D-glucose epimerase. His-79 and His-300 were mutated to prepare the mutants H79L (mutation of histidine to leucine at the 79th amino acid) and H300A (mutation of histidine to alanine at the 300th amino acid) by site-directed mutagenesis. The H79L protein was inactive, showing that His-79 participates in the reaction mechanism.

• BMB Reports
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• v.43 no.6
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• pp.419-426
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• 2010

Aeromonas hydrophila is a bacterial pathogen that infects a large number of eukaryotes, including humans. The UDP-galactose 4'-epimerase (GalE) catalyzes interconversion of UDP-galactose to UDP-glucose and plays a key role in lipopolysaccharide biosynthesis. This makes it an important virulence determinant, and therefore a potential drug target. Our earlier studies revealed that unlike other GalEs, GalE of A. hydrophila exists as a monomer. This uniqueness necessitated elucidation of its structure and active site. Chemical modification of the 6xHis-rGalE demonstrated the role of histidine residue in catalysis and that it did not constitute the substrate binding pocket. Loss of the 6xHis-rGalE activity and coenzyme fluorescence with thiol modifying reagents established the role of two distinct vicinal thiols in catalysis. Chemical modification studies revealed arginine to be essential for catalysis. Site-directed mutagenesis indicated Tyr149 and Lys153 to be involved in catalysis. Use of glycerol as a cosolvent enhanced the GalE thermostability significantly.

• BMB Reports
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• v.35 no.3
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• pp.255-261
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• 2002

GTP cyclohydrolase I (E.C. 3.5.4.16) is a homodecameric protein that catalyzes the conversion of GTP to 7,8-dihydroneopterin triphosphate (H2NTP), the initial step in the biosynthesis of pteridines. It was proposed that the enzyme complex could be composed of a dimer of two pentamers, or a pentamer of tightly associated dimers; then the active site of the enzyme was located at the interface of three monomers (Nar et al. 1995a, b). Using mutant enzymes that were made by site-directed mutagenesis, we showed that a decamer of GTP cyclohydrolase I should be composed of a pentamer of five dimers, and that the active site is located between dimers, as analyzed by a series of size exclusion chromatography and the reconstitution experiment. We also show that the residues Lys 136, Arg139, and Glu152 are of particular importance for the oligomerization of the enzyme complex from five dimers to a decamer.