• Title/Summary/Keyword: chi sequence

Search Result 271, Processing Time 0.027 seconds

An Efficient Method of Remote Control for Select Sequence in Process Control (공정제어에서 선택시퀀스를 위한 효율적인 리모트 콘트롤 제어방법)

  • Kong, Heon-Tag;Kim, Chi-Su;You, Jeong-Bong
    • Journal of the Korea Academia-Industrial cooperation Society
    • /
    • v.11 no.1
    • /
    • pp.107-112
    • /
    • 2010
  • When we design the control system used Programmable Logic controller(PLC), if we program a Sequential Function Chart(SFC), It is easy to understand the sequential flow of control, to maintenance the controller and to describe a program. SFC language is programmed by a single sequence, a select sequence and a parallel sequence. In a select sequence, when the select step is error, the whole process is stopped. If the error step has no connection the whole process, the loss is down when we debugging the program without stopping the whole process. Therefore, this thesis shows the efficient method of remote control for select sequence and we confirmed its feasibility through actual example.

An overview bioactive compounds on the skin of frogs (Anura)

  • Tran Thi Huyen;Phan Thi Hoang Anh;Nguyen Thi Anh Hong;Nguyen Ngoc Duyen;Le Pham Tan Quoc;Tran Dinh Thang
    • Fisheries and Aquatic Sciences
    • /
    • v.26 no.4
    • /
    • pp.241-255
    • /
    • 2023
  • The robust development of frog farming offered high economic benefits but created a large waste residue of frog bones and skin that received little attention. Over the years, inedible by-products have often been processed into biomolecules of potential value and environmental benefits, such as collagen, gelatin, and bioactive peptides. An overview of bioactive compounds on frog skins from various countries indicated that brevinin was the most abundant biological peptide found in frog skin. Other remaining compounds also possessed their highlighted activities, including antibacterial, stimulating insulin release and gastric hormone release, anti-cancer, and neuroregulatory. Notably, various components have been analyzed in the structure and sequence to give meaningful insight into clustering components related to their biological activity. This review may create a source of raw materials for the developmental research of by-products from frog skin and concomitantly reduce environmental pollution.

Functional Role of a Conserved Sequence Motif in the Oxygen-dependent Degradation Domain of Hypoxia-inducible Factor 1α in the Recognition of p53

  • Chi, Seung-Wook
    • Genomics & Informatics
    • /
    • v.6 no.2
    • /
    • pp.72-76
    • /
    • 2008
  • Hypoxia-inducible factor $1{\alpha}\;(HIF1{\alpha})$ is a transcription factor that plays a key role in the adaptation of cells to low oxygen stress and oxygen homeostasis. The oxygen-dependent degradation (ODD) domain of $HIF1{\alpha}$ is responsible for the negative regulation of $HIF1{\alpha}$ in normoxia. The interactions of the $HIF1{\alpha}$ ODD domain with partner proteins such as von Hippel-Lindau tumor suppressor (pVHL) and p53 are mediated by two sequence motifs, the N- and C-terminal ODD(NODD and CODD). Multiple sequence alignment with $HIF1{\alpha}$ homologs from human, monkey, pig, rat, mouse, chicken, frog, and zebrafish has demonstrated that the NODD and CODD motifs have noticeably high conservation of the primary sequence across different species and isoforms. In this study, we carried out molecular dynamics simulation of the structure of the $HIF1{\alpha}$ CODD motif in complex with the p53 DNA-binding domain (DBD). The structure reveals specific functional roles of highly conserved residues in the CODD sequence motif of $HIF1{\alpha}$ for the recognition of p53.

A Study on the Watermarking Methods with Chi-Square Distribution (카이 자승 분포를 이용한 워터마킹기법의 연구)

  • 강환일;김갑일;한승수
    • Proceedings of the Korean Institute of Intelligent Systems Conference
    • /
    • 2001.12a
    • /
    • pp.5-9
    • /
    • 2001
  • In this paper, we propose the new audio watermarking method and can be used on line processing. Instead of the wavelet transform, we use the integer wavelet transform for the reduction of the computational load. The watermark associated with the chi-square distribution is inserted into the signal on the integer wavelet domain. When extracting the watermark, the spread spectrum methods are used with the coefficients associated with the covariance sequence. We show that the chi-square distribution is a good tool for the spread spectrum method on the wavelet domain. This watermarking technique may be used for the control of the electrical product which can be controlled with the hidden signals and can be moved according to the audible signals simultaneously.

  • PDF

Cloning and Sequenece Analysis of the hpa D Gene Responsible for Homoprotocatechuate 2, 3-Dioxgenae from Pseudomonas sp. DJ-12

  • Lee, Sang-Maha;Chae, Jong-Chan;Kim, Young-Soo;Kim, Chi-Kyung
    • Journal of Microbiology
    • /
    • v.39 no.4
    • /
    • pp.334-337
    • /
    • 2001
  • The degradative pathway of homoprotocatechuate (HPC) is the bacterial routhe wherby 3,4-dihydrox-yphenylactic acid is catabolized to pyruvate and succinate by a series of sequential reactions . The HPC is catalzed by homoprotocatechuate 2, 3-dioxygenase(HPC-2,3O) to from 5-carboxymethy1-2-hydroxy-muco semialdehyde. In this study, the hha D gene encoding. HPC, 2, 3O was Cloned from the chromo-somal DNA of Pseudomonas sp. DJ-12 and its nucleotide sequence was analyzed. The open reding frame of hpaD gene was found to be composed of 864 nucleotide pairs and to encode a poypetide with 287 amino acide residues. The deduced amino acid sequence of the HPC-2,3O from Pseudomonas. sp. DJ-12 exhibited 60~64% homology with those of the corresponding enzymes from E. coli. Salmonella enterica, and Klebsiella pneumoniae.

  • PDF

Molecular Cloning and Characterization of 58 kDa Chitinase Gene from Serratia marcescens KCTC 2172

  • Gal Sang Wan;Lee S. W.;Choi Y. J.
    • Biotechnology and Bioprocess Engineering:BBE
    • /
    • v.7 no.1
    • /
    • pp.38-42
    • /
    • 2002
  • A chitinase gene (pCHi58) encoding a 58 kDa chitinase was isolated from the Serratia marcescens KCTC 2172 cosmid library. The chitinase gene consisted of a 1686 bp open reading frame that encoded 562 amino acids. Escherichia coil harboring the pChi58 gene secreted a 58 kDa chitinase into the culture supernatant. The 58 kDa chitinase was purified using a chitin affinity column and mono-S column. A nucleotide and N-terminal amino acid sequence analysis showed that the 58 kDa chitinase had a leader peptide consisting of 23 amino acids which was cleaved prior to the 24th alanine. The 58 KDa chitinase exhibited a $98\%$ similarity to that of S. marcescens OMB 1466 in its nuclotide sequence. The chitinolytic patterns of the 58 kDa chitinase released N,N'-diacetyl chitobiose (NAG2) as the major hydrolysis end-product with a trace amount of N-acetylglucosamine. When a 4-methylumbellyferyl-N-acetylglucosamin monomer, dimmer, and tetramer were used as substrates, the 58 kDa chitinase did not digest the 4-Mu-NAG monomer $(analogue\;of\;NAG_2)$, thereby indicating that the 58 kDa chitinase was likely an endochitinase. The optimum reaction temperature and pH of the enzyme were $50^{\circ}C$ and 5.0, respectively.

The responsibility of C-terminal domain in the thermolabile haemolysin activity of Vibrio parahaemolyticus and inhibition treatments by Phellinus sp. extracts

  • Tran Thi Huyen;Ha Phuong Trang;Nguyen Thi-Ngan;Bui Dinh-Thanh;Le Pham Tan Quoc;Trinh Ngoc Nam
    • Fisheries and Aquatic Sciences
    • /
    • v.26 no.3
    • /
    • pp.204-215
    • /
    • 2023
  • The thermolabile haemolysin (tlh) of Vibrio parahaemolyticus (Vptlh) from V. parahaemolyticus is a multiple-function enzyme, initially describes as a haemolytic factor activated by lecithin and phospholipase A2 enzymatic activity (Shinoda, 1991; Vazquez-Morado, 2021; Yanagase et al., 1970). Until now, the tlh structure has hypothesized including N-terminal and C-terminal domain, but what domain of the Vptlh structure does the haemolytic activity has not been refined yet. In this study, a 450-bp VpTLH nucleotide sequence of the entire Vptlh gene encoded the C-terminal domain cloned firstly to examine its responsibility in the activity of the Vptlh. The C-terminal domain fused with a 6-His-tag named the His-tag-VpC-terminal domain was expressed successfully in soluble form in the BL21 (DE3) PlysS cell. Remarkably, both expression and purification results confirmed a high agreement in the molecular weight of the His-tag-VpC-terminal domain was 47 kDa. This work showed the His-tag-VpC-terminal domain lysed the erythrocyte membranes in the blood agar and the phosphate buffered saline (0.9%) media without adding the lecithin substrate of the phospholipase enzyme. Haemolysis occurred at all tested diluted concentrations of His-tag-VpC-terminal domain (p < 0.05), providing evidence for the independent haemolytic activity of the His-tag-VpC-terminal domain. The content of 100 ㎍ of the His-tag-VpC-terminal domain brought the highest haemolytic activity of 80% compared to that in the three remaining contents. Significantly, the His-tag-VpC-terminal domain demonstrated not to involve the phospholipase activity in Luria-Bertani agar supplemented with 1% (vol/vol) egg yolk emulsion. All results proved the vital responsibility of the His-tag-VpC-terminal domain in causing the haemolytic activity without the required activation by the phospholipase enzyme. Raw extracts of Phellinus igniarus and Phellinus pipi at 10-1 mg/mL inhibited the haemolytic activity of the His-tag-VpC-terminal domain from 67.7% to 87.42%, respectively. Hence applying the His-tag-VpC-terminal domain as a simple biological material to evaluate quickly potential derivatives against the Vptlh in vivo conditions will accessible and more advantageous than using the whole of the Vptlh.

Characterization of the pcbE Gene Encoding 2-Hydroxypenta-2,4-Dienoate Hydratase in Pseudomonas sp. DJ-12

  • Lim, Jong-Chul;Lee, Jeongrai;Jang, Jeong-Duk;Lim, Jai-Yun;Min, Kyung-Rak;Kim, Chi-Kyung;Kim, Young-Soo
    • Archives of Pharmacal Research
    • /
    • v.23 no.2
    • /
    • pp.187-195
    • /
    • 2000
  • Nucleotide sequence extending 2,3-dihydroxybiphenyl 1,2-dioxygenase gene (pcbC) and 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase gene (pcbD) of Pseudomonas sp. DJ-12 was previously analyzed and the two genes were present in the order of pcbD-pcbC preceded by a promoter from Pseudomonas sp. DJ-12. In this study, a 3.8-kb nucleotide sequence located downstream of the pcbC gene was analyzed to have three open reading frames (ORFs) that are designated as orf1, pcbE and orf2 genes. All of the ORFs were preceded by each ribosome-binding sequence of 5-GGAXA-3 (X=G or A). However, no promoter-like sequence and transcription terminator sequence were found in the analyzed region, downstream of pcbC gene. Therefore, the gene cluster appeared to be present in the order of pcbD-pcbC-orf1-pcbE-orf2 as an operon, which is unique organization characterized so far in biphenyl- and PCB-degrading bacteria. The orf1 gene was composed of 1,224 base pairs which can encode a polypeptide of molecular weight 44,950 containing 405 amino acid residues. A deduced amino acid sequence of the orf1 gene product exhibited 21-33% identity with those of indole dioxygenase and phenol hydroxylase components. The pcbE gene was composed of 783 base pairs encoding 2-hydroxypenta-2,4-dienoate hydratase involved in the 4-chlorobiphenyl catabolism. The orf2 gene was composed of 1,017 base pairs encoding a polypeptide of molecular weight 37,378 containing 338 amino acid residues. A deduced amino acid sequence of the orf2 gene product exhibited 31% identity with that of a nitrilotriacetate monooxygenase component.

  • PDF