• 국제학술발표논문집
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• The 6th International Conference on Construction Engineering and Project Management
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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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• 제33권1호
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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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• 제26권3호
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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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• 제35권2호
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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.

• 한국생물정보학회:학술대회논문집
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• 한국생물정보시스템생물학회 2005년도 BIOINFO 2005
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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.

• 생태와환경
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• 제35권4호통권100호
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• pp.266-272
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• 2002

팔당호에 설치된 인공식물섬에서 미생물의 역할을 알아보기 위하여 동물플랑크톤 군집 크기, 총세균수, 활성세균수, ${\beta}$-glucosidase와 phosphatase의 체외효소활성도를 2001년 11월 3일부터 2002년 4월까지 격주로 인공식물섬이 설치된 지역과 바깥지역을 대상으로 조사 분석하였다 인공식물섬 아래에서는 일반적으로 측정하는 환경요인들은 대조구보다 수질이 나쁜 것으로 나타났다. 그러나, 동물 플랑크톤의 수는 대조구보다 굉균 25배, 활성세균의 수는 평균 3-8배, 그리고 체외효소활성도는 훨씬 높은 값을 보였다. 이러한 결과는 인공식물섬에서는 동물플랑크톤-식물플랑크톤-수초-세균의 밀접한 관계가 존재하고, 이 관계에 의하여 동물플랑크톤과 세균의 호흡, 분해작용으로 유기물이 제거되는 것으로 판단되었다.

• 감성과학
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• 제20권2호
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• pp.59-72
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• 2017

수많은 정보의 홍수 속에서 소비자는 자신의 감성에 맞는 스타일을 선택하기 원하므로 개인화 서비스에 대한 효용과 필요성이 꾸준히 증가하고 있다. 본 연구에서는 적극적 개인화 쇼핑몰의 샘플 동영상을 직접 제작하여 인터넷 쇼핑몰 이용자 대학생 170명에 대하여 이를 경험하도록 하였고 이에 따라 소비자 반응이 변하는 것을 측정하였다. 또 소비자의 개인화의 수준에 따라 소비자의 웹사이트 평가, 만족도/인터넷 행동, 제품품질평가 등 반응도 조사하였다. 또한 이를 선호쇼핑몰의 종류, 인터넷 쇼핑몰 접속 횟수에 따라 차이가 존재하는지를 조사하였다. 결과는 첫째, 적극적 개인화 쇼핑몰을 이미 경험해본 대학생 소비자의 경우 적극적 개인화 수준이 높게 나타났다. 선호 쇼핑몰의 종류에 따라서 소극적 개인화 수준이 달랐는데, 일반의류 쇼핑몰을 선호하는 사람들이 낮고 복합대형쇼핑몰과 소셜커머스를 선호하는 사람들은 소극적 개인화 점수가 높았다. 둘째, 대학생 소비자의 적극적 개인화 동영상 경험 전후에 따라서 만족도/인터넷행동, 제품품질 평가는 변화하지 않는 것으로 나타났으나, 소극적 개인화 점수는 감소하고 적극적 개인화 점수와 웹사이트 평가는 증가하는 것으로 나타났다. 셋째, 인터넷 쇼핑몰 접속 횟수는 만족도/인터넷행동, 웹사이트 평가와 정적 상관이 있는 반면에, 적극적 개인화 요소는 만족도/인터넷 행동, 웹사이트 평가와 부적 상관이 있었다.

• BMB Reports
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• 제32권4호
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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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• 제43권6호
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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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• 제35권3호
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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.