• Title/Summary/Keyword: P.E.B frame

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Experimental Study on Structural Performance of Tensile Brace in P.E.B Steel Frames (P.E.B 강골조에서 인장가새의 구조성능에 관한 실험연구)

  • Kim, jong Sung
    • Journal of Korean Society of Steel Construction
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    • v.19 no.5
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    • pp.549-558
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    • 2007
  • Hook bolt brace is being used to construct pre-engineered building's (PEB) systematic frames in steel factory building, but they pose difficulties in terms of their structural performance. There are also few studies on their behavior and there is a need to develop elementary techniques by conducting loading tests on other types of braces (e.g., rod bar, rod shoe, angle), which is used in Japan and the USA. Its structural performance is compared with that of current hook bolt-type brace. Therefore, in this study, we present a basic step in the structural performance of these specimens to examine its performance qualitatively and theof application to PEB frames.

Ultimate strength of long-span buildings with P.E.B (Pre-Engineered Building) system

  • Lee, Seong-Hui;Kim, Young-Ho;Choi, Sung-Mo
    • Steel and Composite Structures
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    • v.19 no.6
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    • pp.1483-1499
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    • 2015
  • With the improvement of the quality of construction materials and the development of construction technologies, large-scale long-span steel frame buildings have been built recently. The P.E.B system using tapered members is being employed as an economically-efficient long-span structure owing to its advantage of being able to distribute stress appropriately depending on the size of sectional areas of members. However, in December 2005 and in February 2014, P.E.B buildings collapsed due to sudden loads such as snow loads and wind gusts. In this study, the design and construction of the P.E.B system in Korea were analyzed and its structural safety was evaluated using the finite element analysis program to suggest how to improve the P.E.B system in order to promote the efficient and rational application of the system.

Characterization of the recombinant cellulase B from Thermotoga maritima (Thermotoga maritima 유래 내열성 cellulase B 융합단백질의 특성 규명)

  • Chung Ho Kim
    • Journal of Applied Biological Chemistry
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    • v.65 no.4
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    • pp.383-386
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    • 2022
  • A gene encoding thermostable cellulase B (TmCelB) was isolated from Thermotoga maritima. The open reading frame (ORF) of TmCelB gene was 825bp long which predicted to encode 274 amino acid residues with a molecular weight of 31,732 Da. The 17 amino acid residues from N-terminal of the TmCelB was known as signal peptides. To analyze the enzymatic activity and biochemical properties, the ORF of TmCelB gene excluding a putative signal sequence encoding 17 amino acids were introduced into the E. coli expression vector, pRSET-B, and overexpressed in E. coli BL21. The optimum temperature of recombinant TmCelB was around 95 ℃, and the optimum pH of recombinant TmCelB was around pH 4.5. The recombinant TmCelB was stable at temperature below 100 ℃.

Cloning and Characterization of Cellulase Gene (cel5B) from Cow Rumen Metagenome

  • Kang, Tae-Ho;Kim, Min-Keun;Barman, Dhirendra Nath;Kim, Jung-Ho;Kim, Hoon;Yun, Han-Dae
    • Journal of agriculture & life science
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    • v.46 no.2
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    • pp.129-137
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    • 2012
  • A carboxymethyl cellulase gene, cel5B, was cloned, sequenced, and expressed in Escherichia coli. pRCS20 in E. coli was identified from metagenomic cosmid library of cow rumen for cellulase activity on a carboxymethyl cellulose agar plates. Cosmid clone (RCS20) was partially digested with Sau3AI, ligated into BamHI site of pBluescript II SK+ vector, and transformed into E. coli $DH5{\alpha}$. The insert DNA of 1.3 kb was obtained, designated cel5B, which has the activity of hydrolyzation of CMC. The cel5B gene had an open reading frame (ORF) of 1,059 bp encoding 352 amino acids with a signal peptide of 48 amino acids and the conserved region, VIYEIYNEPL, belongs to the glycosyl hydrolase family 5. The molecular mass of Cel5B protein expressed from E. coli $DH5{\alpha}$ exhibited to be about 34 kDa by CMC-SDS-PAGE. The optimal pH was 8.0, and the optimal temperature was about $50^{\circ}C$ for its enzymatic activity.

An Active Buffer Management Mechanism to Guarantee the Qos of the Streaming Service in IEEE 802.11e EDCA (IEEE 802.11e EDCA에서 스트리밍 서비스의 QoS 보장을 위한 동적버퍼관리 기술)

  • Lee, Kyu-Hwan;Lee, Hyun-Jin;Kim, Jae-Hyun;Roh, Byeong-Hee
    • The Journal of Korean Institute of Communications and Information Sciences
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    • v.34 no.8B
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    • pp.751-759
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    • 2009
  • Due to the advance of WLAN technology, the use of the multimedia service such as the video streaming service has been increased in the home network. However, we need to study the method which decreases the transmission delay and the frame loss rate to provide QoS of the video streaming service. Therefore, this paper proposes an active buffer management mechanism to guarantee QoS of the streaming service in IEEE 802.11e EDCA. The proposed protocol discards the frame in the HoL of the buffer based on the importance of each frame and the virtual transmission delay of frame newly arriving at the buffer. In the simulation results, the proposed algorithm not only decreases the frame loss probability of important I and P frames but also stabilizes the transmission delay. It may increase the QoS of video streaming services.

Cloning and Characterization of the Tetracycline Resistant Gene, tetB, from Vibrio parahaemolyticus

  • Kang, Min-Seung;Park, Kun-Ba-Wui;Hwang, Hye-Jin;Bae, Hyang-Nam;Lim, Keun-Sik;Eom, Sung-Hwan;Kim, Young-Mog
    • Fisheries and Aquatic Sciences
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    • v.12 no.1
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    • pp.24-28
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    • 2009
  • A tetracycline resistant Vibrio parahaemolyticus, capable of growing on TCBS medium containing tetracycline, was isolated from cultivated fishes. A gene responsible for the tetracycline resistance was cloned from chromosomal DNA of the V. parahaemolyticus strain using Escherichia coli KAM3, which lacks major multi-drug efflux pumps (${\Delta}acrB$) as host cells. The nucleotide sequence and homology analysis revealed an open reading frame (ORF) for tetracycline resistance protein (TetB). In order to characterize the antibiotic resistance of TetB originated from the V. parahaemolyticus strain, the gene was sub cloned into plasmid pSTV28. The resulting plasmid was designated as pSTVTetB and transformated into E. coli KAM3. E. coli KAM3 cells harboring the recombinant plasmid pSTVTetB are able to grow on plates containing tetracycline and oxytetracycline but not doxycycline, indicating that the tetB gene confers the tetracycline- and oxytetracycline-resistance to the host cell.

Secretion of Bacillus subtilis Cytidine Deaminase by the Aid of Signal Sequences in Escherichia coli

  • Yoon, Soo-Ryun;Kim, Sung-Il;Lee, Se-Young;Song, Bang-Ho
    • Journal of Microbiology and Biotechnology
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    • v.1 no.1
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    • pp.22-30
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    • 1991
  • In order to secrete the Bacillus subtilis cytidine deaminase (CDase, cytidine/2'-deoxycytidine deaminase) encoded by the B. subtilis cdd gene in E. coli by the aid of signal sequences, the cdd gene was fused in-frame to either amyE or penP signal sequences and the gene expression and CDase localization were examined. For the penP signal sequence::cdd fusion, the cdd gene with 9 amino acids truncated from the 5'-terminus was fused in-frame to the signal sequence, then the $cdd^{+}$ colonies were not occurred from the minimal plate by cdd complementation. The result suggests that 9 amino acids on the $NH_2-terminal$ of CDase have an essential function in the enzyme activity. The hybrid protein obtained by fused gene amyE signal sequence::cdd structural gene gave $cdd^{+}$ phenotype and about half of the total CDase activity was found to be secreted in the periplasm of E. coli transformant JF611/pSO202. The periplasmic CDase activity of JF611 harboring pSO52 containing the intact cdd gene was considerablely lower than that of the cells harboring pSO202 carrying the hybrid cdd gene. This suggests that the CDase was secreted to the periplasm through the cytoplasmic membrane by the aid of the amyE signal sequence in the E. coli transformant.

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Molecular Analysis and Enzymatic Characterization of Cathepsin B from Olive Flounder (Paralichthys olivaceus) (넙치 카텝신 B의 분자생물학적 분석 및 효소학적 특성 연구)

  • Jo, Hee-Sung;Kim, Na-Young;Lee, Hyung-Ho;Chung, Joon-Ki
    • Journal of Fisheries and Marine Sciences Education
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    • v.26 no.3
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    • pp.543-552
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    • 2014
  • Papain family중 하나인 cysteine protease는 근골격계 질환 치료를 위한target molecule로 인식 되어왔으며 Cathepsin B 는 단백질 분해의 초기과정에 관여하는 cysteine proteases 중 하나이다. 본 연구는 넙치의 cathepsin B 유전자의 발현 양상과 넙치 cathepsin B(PoCtB)의 클로닝, 발현 및 효소특성을 분석하였다. cDNA Library Screening을 이용하여 넙치의 cDNA를 클로닝하였다. 넙치의 동정된 cathepsin B 유전자는 993bp의 open reading frame과 330개의 아미노산으로 이루어져있다. Cathepsin B의 propeptide region 내에 GNFD motif와 occluding loop 가 존재함으로써 이것이 명백하게 cathepsin B group이라는 것을 보여주며, 계통 유전학적 분석 결과 다른 종의 cathepsin B에 비해 초창기에 분화되어 나온 것으로 사료된다. mature enzyme인 maPoCtB은 fusion protein인 glutathione S-transferase를 포함하는 pGEX-4T-1 vector에 삽입하여 E.coli 균주인 $DH5{\alpha}$ 내에 발현시켰다. 재조합 단백질인 PoCtB을 과발현 시킨 결과 53kDa의 분자량을 가진다. 넙치 cathepsin B 활성은 Z-Arg-Arg-AMC와 같은 fluorogenic 펩타이드 기질을 이용하여 측정되었고 적정 pH는 pH.7.5 이다.

A Study on the Design Concepts and Main Construction Processes of the Coal Shed at Thermal Power Plant (화력발전소 석탄저장고 설계개념과 시공과정 상의 주요 공정에 관한 연구)

  • Kim, Si-Hyun;Choi, Jang-Soon
    • Journal of the Korea Academia-Industrial cooperation Society
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    • v.16 no.5
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    • pp.3619-3626
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    • 2015
  • The coal shed at thermal power plant(T.P.P) is the biggest building on size among nuclear, coal and other power plant industry buildings. This the coal shed of indoor type is mass volume, the size of 6 soccer fields and 73 meter in height. Structural and functional elements take priority over aesthetic factors. The shed is built to make mighty space for structural safety and functional store by using the concrete, $75,000m^3$ on the total of central retaining wall and sub buttress, and the steel frame used by 11,744-ton P.E.B. system. The design requirement on its wall and frame, P.E.B. system's feature, and specific data of main process followed by construction are inquired. The aim of this study is to suggest the design requirement and guide for the indoor type of the coal shed.

Molecular Cloning and Sequencing of Cell Wall Hydrolase Gene of an Alkalophilic Bacillus subtilis BL-29

  • Kim, Tae-Ho;Hong, Soon-Duck
    • Journal of Microbiology and Biotechnology
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    • v.7 no.4
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    • pp.223-228
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    • 1997
  • A DNA fragment containing the gene for cell wall hydrolase of alkalophilic Bacillus subtilis BL-29 was cloned into E. coli JM109 using pUC18 as a vector. A recombinant plasmid, designated pCWL45B, was contained in the fragment originating from the alkalophilic B. subtilis BL-29 chromosomal DNA by Southern hybridization analysis. The nucleotide sequence of a 1.6-kb HindIII fragment containing a cell wall hydrolase-encoding gene was determined. The nucleotide sequence revealed an open reading frame (ORF) of 900 bp with a concensus ribosome-binding site located 6 nucleotide upstream from the ATG start codon. The primary amino acid sequence deduced from the nucleotide sequence revealed a putative protein of 299 amino acid residues with an M.W. of 33, 206. Based on comparison of the amino acid sequence of the ORF with amino acid sequences in the GenBank data, it showed significant homology to the sequence of cell wall amidase of the PBSX bacteriophage of B. subtilis.

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