• Title/Summary/Keyword: Circular Buffer

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Data Stream Storing Techniques for Supporting Hybrid Query (하이브리드 질의를 위한 데이터 스트림 저장 기술)

  • Shin, Jae-Jyn;You, Byeong-Seob;Eo, Sang-Hun;Lee, Dong-Wook;Bae, Hae-Young
    • Journal of Korea Multimedia Society
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    • v.10 no.11
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    • pp.1384-1397
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    • 2007
  • This paper proposes fast storage techniques for hybrid query of data streams. DSMS(Data Stream Management System) have been researched for processing data streams that have busting income. To process hybrid query that retrieve both current incoming data streams and past data streams data streams have to be stored into disk. But due to fast input speed of data stream and memory and disk space limitation, the main research is not about querying to stored data streams but about querying to current incoming data streams. Proposed techniques of this paper use circular buffer for maximizing memory utility and for make non blocking insertion possible. Data in a disk is compressed to maximize the number of data in the disk. Through experiences, proposed technique show that bursting insertion is stored fast.

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Effect of Cd Concentration on Characteristics of CdS Thin Films Prepared by Chemical Bath Deposition (화학용액증착법에 의하여 증착된 CdS 박막의 특성에 대한 Cd 농도의 영향)

  • Jung, SungHee;Chung, CheeWon
    • Applied Chemistry for Engineering
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    • v.23 no.4
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    • pp.377-382
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    • 2012
  • CdS thin films have been widely used as a buffer layer of CIGS semiconductor solar cells to reduce the lattice mismatch between transparent electrode and absorber layer. In order to prepare the CdS films with high transparency and low resistivity, they were deposited by varying Cd concentration with the constant S concentration in the solution using chemical bath deposition method. They were analyzed in terms of structural, optical and electrical properties of CdS films according to the $[S^{2-}]/[Cd^{2+}]$ ratio. In the case of Cd concentration higher than S concectration, CdS thin films were formed mainly by cluster- by-cluster formation due to the homogeneous reaction between Cd and S in the solution. Therefore the grain size increased and the transmittance decreased. On the other hand, in the case of Cd concentration lower than S concentration, CdS films were formed by heterogeneous reaction on the substrate rather than in the solution. The CdS films have the grains with the uniform circular shape of a few hundreds ${\AA}$. As the Cd concentration increased in the solution, the $[S^{2-}]/[Cd^{2+}]$ ratio decreased and the resistivity decreased by the increase in the carrier concentration due to the formation S vacancy by the excess Cd.

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

  • Ku Hee-Jung;SEO Jung-Kil;KIM Eun-Hi;HUH Min-Do;CHUNG Joon-Ki;PARK Jang-Su;KANG Shin-Won;PARK Nam Gyu
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.30 no.2
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    • pp.244-251
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    • 1997
  • The relationship between structure and biological activity was studied on the three neuropeptides (mammalian, trout- and goldfish-neuropeptide $\gamma$) that were syntheized by the solid-phase method. Circular dichroism spectra showed that mammalian, trout- and goldfish-neuropeptide $\gamma$ adopted an unordered structure in buffer solution. In the-presence of neutral and acidic liposomes, mammalian and trout-neuropeptioe $\gamma$ also took a random structure. However, goldfish-neuropeptide $\gamma$ took an $\alpha-helical$ structure in acidic liposomes. The intestinal motility response was investigated with carp intestines, guinea-pig ileums and rat duodenums. In case of carp intestine, contractile activity was as follows : goldfish-neuropeptide $\gamma\simeq$ trout-neuropeptide $\gamma>$ mammalian-neuropeptide $\gamma$, On the other hand, the contractile activity of mammalian-neuropeptide $\gamma$ was more potent than trout- and goldfish-neuropeptide $\gamma$ in the guinea-pig ileums and rat duodenums. These results suggest that neuropeptide $\gamma$ show the species-specific activity.

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

  • KIM Eun Jung;SEO Jung-Kil;KIM Chan-Hee;GO Hye-Jin;HUH Min-Do;MOON Jung-Hye;PARK Jang-Su;PARK Nam Gyu
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.32 no.2
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    • pp.232-237
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    • 1999
  • The relationship between structure and contractile activity was studied on the three neuropeptide $\gamma$ (mammalian-, bowfin-, shark-NP$\gamma$) that were synthesized by the solid-phase method. Circular dichroism spectra showed that mammalian-, bowfin- and shark-neuropeptide $\gamma$ took an unordered structure in buffer solution and artificial liposome. The intestinal motility response was investigated with guinea-pig ileum, rat duodenum and carp intestine. In case of carp intestine, contractile activity was as follows; bowfin-NP$\gamma$> shark-NP$\gamma$>mammalian-NP$\gamma$, On the other hand, the contractile activity of mammalian-neuropeptide $\gamma$ was more potent than those of bowfin-, shark-neuropeptide $\gamma$ in the guinea-pig ileum and rat duodenum. These results suggest that NP$\gamma$ show the species-specific activity.

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Circular Buffer Technique for Storing Data Stream (데이터 스트림 저장을 위한 순환버퍼 기법)

  • Shin, Jae-Jyn;You, Byeong-Seob;Eo, Sang-Hun;Lee, Dong-Wook;Bae, Hea-Young
    • Proceedings of the Korea Information Processing Society Conference
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    • 2007.05a
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    • pp.20-23
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    • 2007
  • 본 논문은 데이터 스트림의 저장을 위한 순환버퍼 기법을 제안한다. 빠르고 많은 입력을 가지는 데이터 스트림의 처리를 위해 DSMS(Data Stream Management System)란 새로운 시스템에 대한 연구가 활발히 진행되고 있다. 현재 입력되고 있는 데이터 스트림과 과거에 발생했던 데이터 스트림을 동시에 검색하는 하이브리드 질의를 위해서는 데이터 스트림이 디스크에 저장되어야 한다. 그러나 데이터 스트림의 빠른 입력 속도와 메모리와 디스크 공간의 한계 때문에 저장된 데이터 스트림에 대한 질의보다는, 현재 입력되고 있는 데이터 스트림에 대한 질의에 대한 연구들이 주로 이루어졌다. 본 논문에서는 제안하는 순환버퍼는 데이터 스트림의 입력과 출력을 비동기적으로 빠르게 실행할 수 있다. 또한 입력되는 네트워크 패킷의 감소와 출력 시 디스크 I/O의 감소를 위하여 순환버퍼에서는 데이터 스트림의 묶음 단위로 입출력이 진행된다. 실험을 통하여 기술이 대량으로 입력되는 데이터 스트림을 빠르게 저장시킬 수 있다는 것을 보인다.

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A DESIGN DEVELOPMENT OF 400MHz BAND AUTOCORRELATOR FOR RADIO ASTRONOMY OBSERVATION (우주전파 관측용 400MHz 대역 자기 상관분광기 설계 및 제작)

  • Lee, Chang-Hoon;Choi, Han-Kyu;Kim, Kwang-Dong;Han, Seog-Tae;Kim, Tae-Sung;Byun, Doo-Young;Koo, Bon-Chul
    • Publications of The Korean Astronomical Society
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    • v.18 no.1
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    • pp.51-60
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    • 2003
  • This paper is the research and development including the system design and the prototype system building of the 400MHz wide-band digital autocorrelation spectrometer system for radio astronomy observation, which will be used as back-end signal processing unit of the Dual channel SIS receiver at Taeduk Radio Astronomy Observatory. So in this paper, we performed development of the high speed digitizing sampler, the circular memory buffer, and the correlator module for the 400MHz wide-band digital autocorrelator. This developed system will be use at TRAO after the housing and some calibration.

Purification and Characterization of Cop, a Protein Involved in the Copy Number Control of Plasmid pE194

  • Kwak, Jin-Hwan;Kim, Jung-Ho;Kim, Mu-Yong;Choi, Eung-Chil
    • Archives of Pharmacal Research
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    • v.21 no.3
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    • pp.291-297
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    • 1998
  • Cop protein has been overexpressed in Escherichia coli using a T7 RNA polymerase system. Purification to apparent homogeneity was achieved by the sequential chromatography on ion exchange, affinity chromatography, and reverse phase high performance liquid chromatography system. The molecular weight of the purified Cop was estimated as 6.1 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). But the molecular mass of the native state Cop was shown to be 19 kDa by an analytical high performance size exclusion chromatography, suggesting a trimer-like structure in 50 mM Tris-HCI buffer (pH 7.5) containing 100 mM NaCl. Cop protein Was calculated to contain $39.1% {\alpha}-helix, 16.8% {\beta}-sheet$, 17.4% turn, and 26.8% random structure. The DNA binding property of Cop protein expressed in E. coli Was preserved during the expression and purification process. The isoelectric point of Cop was determined to be 9.0. The results of amino acid composition analysis and N-terminal amino acid sequencing of Cop showed that it has the same amino acid composition and N-terminal amino acid sequence as those deduced from its DNA sequence analysis, except for the partial removal of N-terminal methionine residue by methionyl-aminopeptidase in E. coli.

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Dissolution Enhancements of Tiaprofenic Acid by ${\beta}-Cyclodextrin$ Complexation (${\beta}-Cyclodextrin$과의 복합체 형성에 의한 Tiaprofenic Acid의 용출증가)

  • Chun, In-Koo;Park, In-Sook
    • Journal of Pharmaceutical Investigation
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    • v.16 no.2
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    • pp.55-67
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    • 1986
  • Inclusion complexation of tiaprofenic acid (TPA) with cyclodextrins $({\alpha}-,\;{\beta}-,\;{\gamma}-CyDs)$ in aqueous solution and in solid phase was investigated by solubility method, measurement of partition coefficient, ultra-violet, circular dichroism, infrared spectroscopies, powder X-ray diffractometry and differential scanning calorimetry. Investigations were made to prepare inclusion complexes of TPA with ${\beta}-CyD$ in solid powdered form by coprecipitation, freeze-drying, spray-drying and co-pulverization methods. The coprecipitation, freeze-drying and spray-drying methods were successful in obtaining inclusion complexes. The results showed that the latter two methods might be originally superior to the former in obtaining powdered inclusion completes. Especially, it was shown by powder X-ray diffractometry that spray-dried ${\beta}-CyD$ alone, TPA-spray-dried ${\beta}-CyD$ physical mixture, and spray-dried $TPA-{\beta}-CyD$ complex were amorphous. The dissolution behaviours of $TPA-{\beta}-CyD$ systems prepared by above four methods were compared with those of TPA alone and $TPA-{\beta}-CyD$ physical mixture, and the rates of dissolution of TPA in pH 1.2 buffer were greatly enhanced by inclusion complexation and copulverization.

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Localization of the Membrane Interaction Sites of Pal-like Protein, HI0381 of Haemophilus influenzae

  • Kang, Su-Jin;Park, Sung Jean;Lee, Bong-Jin
    • Molecules and Cells
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    • v.26 no.2
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    • pp.206-211
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    • 2008
  • HI0381 of Haemophilus influenzae was investigated by circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy. HI0381 is a 153-residue peptidoglycan-associated outer membrane lipoprotein, and a part of the larger Tol/Pal network. Here, we report its backbone $^1H$, $^{15}N$, and $^{13}C$ resonance assignments, and secondary structure predictions. About 97% of all of the $^1HN$, $^{15}N$, $^{13}CO$, $^{13}C{\alpha}$, and $^{13}C{\beta}$ resonances covering 131 non-proline residues of the 134 residue, mature protein, were clarified by sequential and specific assignments. CSI and TALOS analyses revealed that HI0381 contains five ${\alpha}$-helices and five ${\beta}$-strands. To characterize the structure of HI0381, the effects of pH and salt concentration were investigated by CD. In addition, the structural changes occurring when HI0381 was in a membranous environment were investigated by comparing its HSQC spectra and CD data in buffer and in DPC micelles; the results showed that helix ${\alpha}4$ and strand ${\beta}4$ became aligned with the membrane. We conclude that the conformation of HI0381 is affected by the membrane environment, implying that its folded state is directly related to its function.

Binding Characteristics to Mosquito-larval Midgut Proteins of the Cloned Domain II-III Fragment from the Bacillus thuringiensis Cry4Ba Toxin

  • Moonsom, Seangdeun;Chaisri, Urai;Kasinrerk, Watchara;Angsuthanasombat, Chanan
    • BMB Reports
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    • v.40 no.5
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    • pp.783-790
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    • 2007
  • Receptor binding plays an important role in determining host specificity of the Bacillus thuringiensis Cry $\delta$-endotoxins. Mutations in domains II and III have suggested the participation of certain residues in receptor recognition and insect specificity. In the present study, we expressed the cloned domain II-III fragment of Cry4Ba and examined its binding characteristics to mosquito-larval midgut proteins. The 43-kDa Cry4Ba-domain II-III protein over-expressed in Escherichia coli as inclusion bodies was only soluble when carbonate buffer, pH 10.0 was supplemented with 4M urea. After renaturation via stepwise dialysis and subsequent purification, the refolded domain II-III protein, which specifically reacts with anti Cry4Ba-domain III monoclonal antibody, predominantly exists as a $\beta$-sheet structure determined by circular dichroism spectroscopy. In vitro binding analysis to both histological midgut tissue sections and brush border membrane proteins prepared from susceptible Aedes aegypti mosquito-larvae revealed that the isolated Cry4Ba-domain II-III protein showed binding functionality comparable to the 65-kDa full-length active toxin. Altogether, the data present the 43-kDa Cry4Ba fragment comprising domains II and III that was produced in isolation was able to retain its receptor-binding characteristics to the target larval midgut proteins.