• 제목/요약/키워드: ${\gamma}/{\gamma}'$ structure

검색결과 701건 처리시간 0.027초

${\gamma}$-FUZZY FILTER AND LIMIT STRUCTURE

  • Lee, Yoon-Jin
    • 한국지능시스템학회:학술대회논문집
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    • 한국퍼지및지능시스템학회 1998년도 The Third Asian Fuzzy Systems Symposium
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    • pp.219-224
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    • 1998
  • We introduce the notion of ${\gamma}$-fuzzy filter and ${\gamma}$-limit structure to L-fuzzy point. We show that the category ${\gamma}$Lim of ${\gamma}$-limit spaces is a cartesian closed topological construct containing the category LFTop of stratified L-fuzzy topological spaces as a bireflective subcategory.

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Neuropeptide $\gamma$의 구조 및 생리활성 (Conformation and Biological Activity of the Neuropeptide $\gamma$)

  • 구희정;서정길;김은희;허민도;정준기;박장수;강신원;박남규
    • 한국수산과학회지
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    • 제30권2호
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    • pp.244-251
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    • 1997
  • 생리활성을 지닌 신경펩타이드의 구조와 활성간의 관계를 규명하기 위하여 고상법으로 합성한 세 종류의 neuropeptide $\gamma$(mammalian-, trout- 그리고 goldfish-neu-ropeptide $\gamma$)를 사용하여 연구하였다. Circular dichroism spectra에 의하면 mammalian-, trout-와 goldfish-neurope-ptide $\gamma$는 완충액 조건하에서 모두 random한 구조를 나타내었다. 중성 및 산성 지질 존재 하에서, mammalian과 trout-neuropeptide $\gamma$는 여전히 random한 구조를 취했다. 그러나, goldfish-neuropeptide $\gamma$는 중성 및 산성지질하에서 부분적으로 $\alpha-helix$ 구조를 나타내었다. 장관 수축활성 에 있어서는 carp 장관, guinea-pig 회장 그리고 rat 십이지장에 대하여 비교하였다. Carp에 대해서는 goldfish-neuropeptide $\gamma\;\simeq$ trout-neuropeptide $\gamma\;>$ mammalian- neuropeptide $\gamma$ 순으로 활성이 나타났다. 그러나, guinea-pig 회장과 rat 십이지장에 대해서 mammalian-neuropeptide $\gamma$는 어류 유래성 neuropeptide g들 보다 높은 수축활성을 나타내었다. 이러한 결과들은 neuropeptide $\gamma$들이 종-특이적인 활성을 나타낸다는 것을 제시한다.

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닭 인터페론 유전자의 클로닝에 관한 연구 (MOLECULAR CLONING OF CHICKEN INTERFERON-GAMMA)

  • 송기덕;;한재용
    • 한국가금학회:학술대회논문집
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    • 한국가금학회 1999년도 제16차 정기총회및학술발표회
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    • pp.34-50
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    • 1999
  • A cDNA encoding chicken interferon-gamma (chIFN-${\gamma}$) was amplified from P34, a CD4$^{+}$ T-cell hybridoma by reverse transcription-polymerase chain reaction (RT-PCR) and cloned into pUC18. THe sequences of cloned PCR products were determined to confirm the correct cloning. Using this cDNA as probe, chicken genomic library from White Leghorn spleen was screened. Phage clones harboring chicken interferon-gamma (chIFN-${\gamma}$) were isolated and their genomic structure elucidated. The chIFN-${\gamma}$ contains 4 exons and 3 introns spanning over 14 kb, and follows the GT/AG rule for correct splicing at the exon/intron boundaries. The four exons encode 41, 26, 57 and 40 amino acids, respectively, suggesting that the overall structure of IFN-${\gamma}$ is evolutionairly conserved in mammalian and avian species. The 5’-untranslated region and signal sequences are located in exon 1. Several AT-rich sequences located in the fourth exon may indicate a role in mRNA turnover. The 5’-flanking region contains sequences homologous to the potential binding sites for the mammalian transcription factors, activator protein-1(AP-1) activator protein-2(AP-2) cAMP-response element binding protein(CREB), activating transcription factor(ATF), GATA-binding fator(GATA), upstream stimulating factor(USF), This suggests that the mechanisms underlying transcriptional regulation of chicken and mammalian IFN-${\gamma}$ genes may be similar.r.

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Bowfin-과 Shark-neuropeptide $\gamma$의 구조 및 수축효과 (Structure and Contractile Activity of the Bowfin- and Shark-neuropeptide $\gamma$)

  • 김은정;서정길;김찬희;고혜진;허민도;문정혜;박장수;박남규
    • 한국수산과학회지
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    • 제32권2호
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    • pp.232-237
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    • 1999
  • Tachykinin peptide의 구조와 생리활성간의 상관관계를 조사하기 위해 고상법으로 합성한 어류 유래의 neuropeptide $\gamma$(Mammalian-, Bowfin- 그리고 Shark-neuropeptide $\gamma$)를 사용하였다. 이들의 이차 구조를 알아보기 위해 circular dichroism (CD)을 이용하였다. CD 연구 결과에 따르면, mammalian-neuropeptide $\gamma$, bowfin-neuropeptide $\gamma$와 shark-neuropeptide $\gamma$는 완충액과 인공지질막 조건하에서 random구조를 나타내었다. 또한 이들 neuropeptide $\gamma$의 장관에 대한 수축 활성을 조사하기 위해 guinea-pig의 회장, rat의 십이지장과 carp intestine을 사용하였다. Carp intestine에 서 bowfin-neuropeptide $\gamma$>shark- neuropeptide $\gamma$>mammalian-neuropeptide $\gamma$순으로 활성 이 나타났다. 그러나, guinea-pig 회장과 rat 십이지장에 대해서 mammalian-NP$\gamma$의 활성이 어류 유래의 neuropeptide $\gamma$들보다 높게 나타났다. 이러한 결과들은 neuropeptide $\gamma$가 종-특이적인 활성을 나타냄을 제시한다.

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CMSX-10 단결정 초내열합금에서 거시편석에 따른 γ/γ' 응고조직 형성 (Investigation of γ/γ' Growth by Macro Segregation in the Ni-Base Single Crystal Superalloy, CMSX-10)

  • 윤혜영;성창훈;신종호;한승전;이재현
    • 한국재료학회지
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    • 제25권9호
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    • pp.435-441
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    • 2015
  • The ${\gamma}/{\gamma}^{\prime}$ two-phases, commonly known as a eutectic structure, are observed in the ${\gamma}$ interdendritic region of a Ni-base superalloy. However, the growth behavior of the ${\gamma}/{\gamma}^{\prime}$ two-phases, whether it is of eutectic or peritectic nature, has not been decidedly established. Directional solidifications were, thus, performed with the planar interface at a low growth rate of $0.5{\mu}m/s$ in order to promote macro segregation. Directional solidification started with the ${\gamma}$ planar interface and the ${\gamma}^{\prime}$ phase nucleated on the ${\gamma}$ planar interface at the solidification fraction of 0.75. The ${\gamma}/{\gamma}^{\prime}$ two-phases showed the ${\gamma}^{\prime}$ rod structure as major phase and the ${\gamma}$ minor phase between ${\gamma}^{\prime}$ rods, and the volume fraction of the ${\gamma}$ phase changed continuously with an increasing solidification fraction. The two-phase ${\gamma}/{\gamma}^{\prime}$ is seen as the coupled peritectic.

글루타치온 생산효소( $\gamma$-Glutamylcysteine Synthetase)와 그 변이효소의 구조분석 및 반응 Kinetics 연구

  • 양혜정;권대영
    • 식품기술
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    • 제17권4호
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    • pp.98-106
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    • 2004
  • Two mutant enzymes of $\gamma$-glutamylcysteine synthetase ($\gamma$-GCS) which catalyzed the synthesis of $\gamma$-glutamylcysteine from L-glutamic acid and L-cysteine in the presence of ATP, were prepared bypoint mutation of $\gamma$-GCS gene with site-directed mutagensis in E. coli. Conformational structuresand catalytic reaction kinetics of mutant enzymes were compared with wild type $\gamma$-GCS afterpurification. The S495F mutant enzyme (serine at 495 residue was substituted with phenylalanine),which had no catalytic activity for $\gamma$-glutamylcysteine synthesis, rarely folded even in neutral pH.However, the mutant A494V (alanine of 494 residue was replaced by valnine) which showed 50 %increase of activity, had a high folding structure. The folding structure of A494V also more stable athigh temperature and extreme pH compared to wild type and S495F. Reaction kinetics of wild typeand A494V were also investigated, Km value of A494V was smaller than that of wild type, while itshowed a little difference at Vmax values. This result evolved that alanine at 494 may be involved inbinding site of substrate rather than catalytic site. In addition, change of catalytic activity by onepoint mutation was highly correlated with the folding structure of enzyme.

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STRUCTURES OF INVOLUTION Γ-SEMIHYPERGROUPS

  • Yaqoob, Naveed;Tang, Jian;Chinram, Ronnason
    • 호남수학학술지
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    • 제40권1호
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    • pp.109-124
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    • 2018
  • In this paper, structure of involution ${\Gamma}$-semihypergroup is introduced and some theorems about this concept are stated and proved. The concept of ${\Gamma}$-hyperideal in involution ${\Gamma}$-semihypergroup is defined and some of their properties are studied. Some results on regular ${\Gamma}^*$-semihypergroups and fuzzy ${\Gamma}^*$-semihypergroups are also provided.

Solution Structure of Neuropeptide $\gamma$ from Carassius auratus by NMR spectroscopy

  • Lee, Sangwon;Park, Namgyu;Kim, Yangmee
    • 한국생물물리학회:학술대회논문집
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    • 한국생물물리학회 1999년도 학술발표회 진행표 및 논문초록
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    • pp.31-31
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    • 1999
  • Neuropeptide ${\gamma}$ is a recently identified tachykinin family peptide which has conserved ammo acid sequence of -Phe-X-Gly-Leu-Met-NH2 in the C-terminal region, where X represents aromatic or hydrophobic residues. In this study, three-dimensional structure of neuropeptide ${\gamma}$ from goldfish Carassius auratus (G-NP${\gamma}$) was determined by NMR spectroscopy.(omitted)

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Effect of Gamma-Irradiation on the Molecular Properties of Blood Plasma Proteins

  • Song, Kyung-Bin;Lee, Seunghwan;Lee, Seunghyun
    • Preventive Nutrition and Food Science
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    • 제7권2호
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    • pp.184-187
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    • 2002
  • Blood products from slaughterhouses that are not hygienically prepared for disposal or food consumption pose a human health hazard. Gamma irradiation is an effective method for sterilization of blood products, but may introduce changes in the molecular characteristics of proteins. This study evaluated the effects of irradiation on animal plasma proteins. Bovine and porcine blood was obtained from a slaughterhouse and the plasma proteins purified and lyophilized. The secondary structure and molecular weight distribution of the plasma protein solutions and powders were examined after ${\gamma}$-irradiation at 1, 5, 7 and 10 kGy. Gamma-irradiation affected the molecular properties of the protein solutions, but not the protein powders. Circular dichroism and sodium dodecyl sulfate-polyacrylamide gel electrophoresis studies showed that increased doses of ${\gamma}$-irradiation decrease the ordered structure of plasma proteins in solution, and cause initial fragmentation of the polypeptide chains and subsequent aggregation.

The crystal and molecular structure of $\gamma$-hydroxy-.$\beta$-amino butyric acid

  • Kim, Yang-Bae
    • Archives of Pharmacal Research
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    • 제8권1호
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    • pp.1-6
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    • 1985
  • The crystal structure or $\gamma$-hydroxy-$\betha$-aminobutyric acid was determined by MULTAN system with X-ray intensity data on a diffractometer and refined by the least-squares method to an R-value 0.034 for 711 reflections. The crystals were orthorhombic, space group $P2_{1}2_{1}2_{1}$, Z = 4, with a = 10.220, b = 8.257 and c = 6.556$\AA$. The molecule takes the zwitterionic form and skeletal conformation is trans-transform. The molecules are held together by intra-and intermolecular NH-O and OH--O hydrogen bonds.

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