• 제목/요약/키워드: Research Domain

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Exploring Cross-function Domain Interaction Map

  • Li, Xiao-Li;Tan, Soon-Heng;Ng, See-Kiong
    • 한국생물정보학회:학술대회논문집
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    • 한국생물정보시스템생물학회 2005년도 BIOINFO 2005
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    • pp.431-436
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    • 2005
  • Living cells are sustained not by individual activities but rather by coordinated summative efforts of different biological functional modules. While recent research works have focused largely on finding individual functional modules, this paper attempts to explore the connections or relationships between different cellular functions through cross-function domain interaction maps. Exploring such a domain interaction map can help understand the underlying inter-function communication mechanisms. To construct a cross-function domain interaction map from existing genome-wide protein-protein interaction datasets, we propose a two-step procedure. First, we infer conserved domain-domain interactions from genome-wide protein-protein interactions of yeast, worm and fly. We then build a cross-function domain interaction map that shows the connections of different functions through various conserved domain interactions. The domain interaction maps reveal that conserved domain-domain interactions can be found in most detected cross-functional relationships and a f9w domains play pivotal roles in these relationships. Another important discovery in the paper is that conserved domains correspond to highly connected protein hubs that connect different functional modules together.

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A Prior Model of Structural SVMs for Domain Adaptation

  • Lee, Chang-Ki;Jang, Myung-Gil
    • ETRI Journal
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    • 제33권5호
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    • pp.712-719
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    • 2011
  • In this paper, we study the problem of domain adaptation for structural support vector machines (SVMs). We consider a number of domain adaptation approaches for structural SVMs and evaluate them on named entity recognition, part-of-speech tagging, and sentiment classification problems. Finally, we show that a prior model for structural SVMs outperforms other domain adaptation approaches in most cases. Moreover, the training time for this prior model is reduced compared to other domain adaptation methods with improvements in performance.

Domain Analysis of Device Drivers Using Code Clone Detection Method

  • Ma, Yu-Seung;Woo, Duk-Kyun
    • ETRI Journal
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    • 제30권3호
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    • pp.394-402
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    • 2008
  • Domain analysis is the process of analyzing related software systems in a domain to find their common and variable parts. In the case of device drivers, they are highly suitable for domain analysis because device drivers of the same domain are implemented similarly for each device and each system that they support. Considering this characteristic, this paper introduces a new approach to the domain analysis of device drivers. Our method uses a code clone detection technique to extract similarity among device drivers of the same domain. To examine the applicability of our method, we investigated whole device drivers of a Linux source. Results showed that many reusable similar codes can be discerned by the code clone detection method. We also investigated if our method is applicable to other kernel sources. However, the results show that the code clone detection method is not useful for the domain analysis of all kernel sources. That is, the applicability of the code clone detection method to domain analysis is a peculiar feature of device drivers.

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SCA에서 적응형 도메인 프로파일 파서의 구축 방법 (Construction of a Adaptive Domain Profile Parser in the SCA)

  • 배명남;이병복;박애순;이인환;김내수
    • 전자공학회논문지CI
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    • 제46권1호
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    • pp.103-111
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    • 2009
  • SCA에서 코어 프레임워크는 이동단말 플랫폼의 시동, 무선의 초기화 등의 시점에 도메인 프로파일을 파싱하고, 이에 따라 플랫폼을 재구성하는 일종의 미들웨어이다. 도메인 프로파일은 XML로 작성되며, 소프트웨어 컴포넌트와 하드웨어 장치에 대한 고유 특성들을 포함하고 있다. 기본적으로, 코어 프레임워크는 도메인 프로 일을 파싱하기 위해 도메인 프로파일 파서를 포함해야 한다. 본 논문은 도메인 프로파일 파서를 구축하는 방법에 있어서, 이동단말과 같은 제한된 환경에도 적용할 수 있도록 도메인 프로파일 파서를 경량화하고, XML 파서 벤더에 대한 독립성을 강화하는 방법을 제안하고자 한다. 이를 통해, 도메인 프로파일 파서는 도메인 프로파일의 반복적인 파싱으로 인한 DOM 트리 생성에 대한 오버헤드 문제, 특정 XML 파서 벤더에 의한 호환성 저하 문제, 도메인 프로파일 기술 방식에 대한 의존성 문제 등을 해결할 수 있다.

Structure of the Starch-Binding Domain of Bacillus cereus $\beta-Amylase$

  • Yoon, Hye-Jin;Akira, Hirata;Motoyasu, Adachi;Atsushi, Sekine;Shigeru, Utsumi;Bunzo, Mikami
    • Journal of Microbiology and Biotechnology
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    • 제9권5호
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    • pp.619-623
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    • 1999
  • The C-terminal starch-binding domain of Bacillus cereus $\beta$-amylase expressed in Escherichia coli was purified and crystallized using the vapor diffusion method. The crystals obtained belong to a space group of $P3_2$ 21 with cell dimensions, a=b=60.20${\AA},\; c=64.92{\AA},\; and \; \gamma = 120^{\circ}$ The structure was determined by the molecular replacement method and refined at 1.95 ${\AA}$, with R-factors of 0.181. The final model of the starch-binding domain comprised 99 amino acid residues and 108 water molecules. The starch-binding domain had a secondary structure of two 4-stranded antiparallel p-sheets similar to domain E of cyclodextrin glucanotransferase and the C-terminal starch-binding domain of glucoamylase. A comparison of the structures of these starch-binding domains revealed that the separated starch-binding domain of Bacillus cereus $\beta-Amylase$had only one starch-binding site (site 1) in contrast to two sites (site 1 and site 2) reported in the domains of cyclodextrin glucanotransferase and glucoamylase.

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Expression and Biochemical Characterization of the Periplasmic Domain of Bacterial Outer Membrane Porin TdeA

  • Kim, Seul-Ki;Yum, Soo-Hwan;Jo, Wol-Soon;Lee, Bok-Luel;Jeong, Min-Ho;Ha, Nam-Chul
    • Journal of Microbiology and Biotechnology
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    • 제18권5호
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    • pp.845-851
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    • 2008
  • TolC is an outer membrane porin protein and an essential component of drug efflux and type-I secretion systems in Gram-negative bacteria. TolC comprises a periplasmic $\alpha$-helical barrel domain and a membrane-embedded $\beta$-barrel domain. TdeA, a functional and structural homolog of TolC, is required for toxin and drug export in the pathogenic oral bacterium Actinobacillus actinomycetemcomitans. Here, we report the expression of the periplasmic domain of TdeA as a soluble protein by substitution of the membrane-embedded domain with short linkers, which enabled us to purify the protein in the absence of detergent. We confirmed the structural integrity of the TdeA periplasmic domain by size-exclusion chromatography, circular dichroism spectroscopy, and electron microscopy, which together showed that the periplasmic domain of the TolC protein family fold correctly on its own. We further demonstrated that the periplasmic domain of TdeA interacts with peptidoglycans of the bacterial cell wall, which supports the idea that completely folded TolC family proteins traverse the peptidoglycan layer to interact with inner membrane transporters.

A Method and Tool for Identifying Domain Components Using Object Usage Information

  • Lee, Woo-Jin;Kwon, Oh-Cheon;Kim, Min-Jung;Shin, Gyu-Sang
    • ETRI Journal
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    • 제25권2호
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    • pp.121-132
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    • 2003
  • To enhance the productivity of software development and accelerate time to market, software developers have recently paid more attention to a component-based development (CBD) approach due to the benefits of component reuse. Among CBD processes, the identification of reusable components is a key but difficult process. Currently, component identification depends mainly on the intuition and experience of domain experts. In addition, there are few systematic methods or tools for component identification that enable domain experts to identify reusable components. This paper presents a systematic method and its tool called a component identifier that identifies software components by using object-oriented domain information, namely, use case models, domain object models, and sequence diagrams. To illustrate our method, we use the component identifier to identify candidates of reusable components from the object-oriented domain models of a banking system. The component identifier enables domain experts to easily identify reusable components by assisting and automating identification processes in an earlier development phase.

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Thickness-dependent magnetic domain structures of Co ultra-thin film investigated by scanning transmission X-ray microscopy

  • Yoon, Ji-Soo;Kim, Namdong;Moon, Kyoung-Woong;Lee, Joo In;Kim, Jae-Sung;Shin, Hyun-Joon;Kim, Wondong
    • Current Applied Physics
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    • 제18권11호
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    • pp.1185-1189
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    • 2018
  • Thickness-dependent magnetic domain structure of ultrathin Co wedge films (0.3 nm-1.0 nm) sandwiched by Pt layers was investigated by scanning transmission x-ray microscopy (STXM) employing X-ray magnetic circular dichroism (XMCD), utilizing elliptically polarized soft x-rays and electromagnetic fields, with a spatial resolution of 50 nm. The magnetic domain images measured at the Co $L_3$ edge showed the evolution of the magnetic domain structures from maze-like form to the bubble-like form as the perpendicular magnetic field was applied. The asymmetric domain expansion of a 500 nm-scale bubble domain was also measured when the in-plane and perpendicular external magnetic field were applied simultaneously.

Purification and Spectroscopic Characterization of the Human Protein Tyrosine Kinase-6 SH3 Domain

  • Koo, Bon-Kyung;Kim, Min-Hyung;Lee, Seung-Taek;Lee, Weon-Tae
    • BMB Reports
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    • 제35권3호
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    • pp.343-347
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    • 2002
  • The human protein tyrosine kinase-6 (PTK6) polypeptide that is deduced from the cDNA sequence contains a Src homology (SH) 3 domain, SH2 domain, and catalytic domain of tyrosine kinase. We initiated biochemical and NMR characterization of PTK6 SH3 domain in order to correlate the structural role of the PTK6 using circular dichroism and heteronuclear NMR techniques. The circular dichroism data suggested that the secondary structural elements of the SH3 domain are mainly composed of $\beta$-sheet conformations. It is most stable when the pH is neutral based on the pH titration data. In addition, a number of cross peaks at the low-field area of the proton chemical shift of the NMR spectra indicated that the PTK6 SH3 domain retains a unique and folded conformation at the neutral pH condition. For other pH conditions, the SH3 domain became unstable and aggregated during NMR measurements, indicating that the structural stability is very sensitive to pH environments. Both the NMR and circular dichroism data indicate that the PTK6 SH3 domain experiences a conformational instability, even in an aqueous solution.

Integrated Effect of Domain and Entrepreneurial Passion on Innovation Strategies of Independently Owned Restaurants: Evidence from Pakistan

  • AZIZ, Rabia;KANG, Shinhyung
    • 융합경영연구
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    • 제9권6호
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    • pp.1-13
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    • 2021
  • Purpose: This research explores how domain passion in addition to entrepreneurial passion influences innovation strategy of venture, thus expanding the role of passion in choosing the path for innovation strategy. Passion is considered one of the most debated concepts in entrepreneurship, psychology, and marketing literatures, and yet a framework describing the integrated effect of entrepreneurial and domain passion on innovation strategy of venture is still lacking. Research data and methodology: Based on an inductive qualitative approach, the research addresses these issues via analyzing four unique cases of independently owned restaurants in Pakistan. The research focusses on the entrepreneurs who startup a venture out of a passion for a specific domain and have a passion for entrepreneurship either from start or it fuels up later during entrepreneurial process. Results: In the presence of both types of passions (Domain and entrepreneurial), the individuals will be inclined towards ambidexterity which differ in types from case to case according to different combinations and intensities (harmonious and obsessive) of passion. Conclusion: Research shows how innovation strategy of domain passion driven ventures is influenced by both entrepreneurial and domain passion, so to understand the role of passion in such cases integrated effect of both passions needs to be explored.