• Molecules and Cells
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• 제25권1호
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• pp.138-141
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• 2008

HP0892 (SwissProt/TrEMBL ID O25552) is a 90-residue conserved hypothetical protein from Helicobacter pylori strain 26695, with a calculated pI of 9.38 and a molecular mass of 10.41 kDa. It belongs to the Plasmid stabilization system protein family (PF05016) in the Pfam database. Proteins with sequence similarity to HP0892 exist in Vibrio choierae, Enterococcus faecalis, Campylobacter jejuni, Streptococcus pneumoniae, Haemophilus influenzae, Escherichia coli O157. Here we report the sequence-specific backbone resonance assignments of HP0892 using multidimentional heteronuclear NMR spectroscopy. About 97.0% (422/435) of the HN, N, CO, $C{\beta}$, $C{\alpha}$ resonances of 90 residues of HP0892 were assigned. On the basis of the resonance assignments, three helical regions and four strand regions were identified using the CSI program. This study is a prerequisite for calculating the solution structure of HP0892, and will be useful for studying its interaction with other molecules.

• 한국통신학회논문지
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• 제27권5C호
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• pp.422-434
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• 2002

본 논문에서는 대용량 트래픽의 효율적 전송을 위해 B-DCS(Broadband-Digital Cross-connect System)망, 간선링, 지선링의 3계위 구조 광섬유 기간전송망을 제안하며 각 계위에서 경제적으로 망의 생존도를 보장하는 설계방법을 연구한다. 링 구축비용을 혼합정수계획(MIP) 모델을 이용해 수리적으로 최적화할 경우 비다항식 완전 문제(NP-complete problem)가 되어 실시간 내에 해를 구하기가 어려워지므로 본 논문에서는 B-DCS망을 위한 운용회선 및 예비회선의 최적할당 문제, 간선링을 위한 다중링 부하최적화 문제, 지선링을 위한 중첩링 부하최적화 문제에 대한 휴리스틱 알고리즘을 각각 개발하여 사례분석을 통해 그 효용성을 보인다.

• Molecules and Cells
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• 제20권3호
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• pp.442-445
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• 2005

HP0894 (SwissProt/TrEMBL ID O25554) is an 88-residue conserved hypothetical protein from Helicobacter pylori strain 26695 with a calculated pI of 8.5 and a molecular weight of 10.38 kDa. Proteins with sequence similarity to HP0894 exist in Vibrio choierae, Enterococcus faecalis, Campylobacter jejuni, Streptococcus pneumoniae, Haemophilus influenzae, Escherichia coli O157, etc. Here we report the sequence-specific backbone resonance assignments of HP0894. About 97.5% (418/429) of the HN, N, CO, $C{\alpha}$, $C{\beta}$ resonances of the 88 residues of HP0894 were assigned. On the basis of these assignments, three helical regions and four strand regions were identified using the CSI program. This study is a prerequisite for calculating the solution structure of HP0894, and studying its interaction with its substrates, if any, and/or with other proteins.

• 한국자기공명학회논문지
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• 제25권3호
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• pp.39-44
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• 2021

The CRISPR-Cas system provides adaptive immunity for bacteria and archaea against invading phages and foreign plasmids. In the Class 1 CRISPR-Cas system, multi-subunit Cas proteins assemble with crRNA to bind to DNA targets. To disarm the bacterial defense system, bacteriophages evolved anti-CRISPR (Acr) proteins that actively inhibit the host CRISPR-Cas function. Here we report the backbone resonance assignments of AcrIF7 protein that inhibits the type I-F CRISPR-Cas system of Pseudomonas aeruginosa using triple-resonance nuclear magnetic resonance spectroscopy. We employed various computational methods to predict the structure and binding interface of AcrIF7, and assessed the model with experimental data. AcrIF7 binds to Cas8f protein via flexible loop regions to inhibit target DNA binding, suggesting that conformational heterogeneity is important for the Cas-Acr interaction.

• 한국정보과학회:학술대회논문집
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• 한국정보과학회 1998년도 가을 학술발표논문집 Vol.25 No.2 (3)
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• pp.483-485
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• 1998

6Bone(IPv6 Backbone)은 IPv6 환경의 개발 촉진 및 진화를 위해 만든 전세계적인 실험망이다. 본 논문은 국내 6Bone인 6Bone KR의 구축을 위해 주소 할당 및 라우팅 규칙을 정의한 내용을 기술한다. 기존의 6Bone 주소 구조를 알아보고, 6Bone KR의 주소 체계가 어떻게 기존의 6Bon을 따르면서, 6Bone KR의 계층적 전개를 위한 연결 규칙을 가지는 가를 살펴본다. 그리고 현재 6Bone KR이 구성된 상황과 개발한 연결 테스트의 프로그램을 소개한다. 이밖에 6Bone KR진화를 위한 몇 가지 고려사항들을 분석하고, 이것을 기반으로 Renumbering을 이용한 새로운 이동 IPv6 환경을 제안한다.

• 한국멀티미디어학회논문지
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• 제14권5호
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• pp.658-668
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• 2011

지난 수 십 년간 통신 기술의 발전과 웹 서비스의 팽창은 인터넷 사용자 수의 폭발적인 증가와 화상회의, 가상 증감 현실, 인터넷 게임 등 실시간 멀티미디어 멀티캐스트 서비스의 급격한 증가를 초래했다. 고밀도 파장분할다중화기술에 기반한 DWDM(Dense-Wavelength Division Multiplexing) 기술은 인터넷 사용자의 증가와 그에 따른 대역폭 요구를 수용하기 위한 방안으로 국가나 글로벌 영역 범위의 차세대 인터넷망 구현을 위한 백본망 기술로 여겨지며, 이러한 DWDM 전달망에서는 멀티캐스트 연결 요구에 대해 최적의 경로를 선택하고 선택된 경로에 효율적으로 파장을 할당하는 멀티캐스트 RWA(Routing and Wavelength Assignment) 문제가 파장 대역폭의 효율적인 활용 측면에서 매우 중요하게 다루어지고 있다. 주어진 파장 수 환경에서 최대한 많은 수의 멀티캐스트 연결을 달성하는 문제는 일반적으로 Non -deterministic Polynomial-time-complete 문제로 여겨지는 데, 본 논문에서는 가상소스를 기반으로 노드의 능력에 따른 차등화로 우선 순위를 적용하여 휴리스틱하게 멀티캐스트 라우팅 경로를 효율적으로 선정하는 DVS-PMIPMR (Differentiated Virtual Source-based Priority Minimum Interference Path Multicast Routing) 알고리즘을 제안한다. 마지막으로 같은 조건에서 더 많은 수의 멀티캐스트 라우팅 패스의 연결이 가능함을 시뮬레이션 및 성능분석 증명한다.

• BMB Reports
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• 제36권5호
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• pp.505-507
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• 2003

One of the small proteins from Helicobacter pylori, acyl carrier protein (ACP), was investigated by NMR. ACP is related to various cellular processes, especially with the biosynthesis of fatty acid. The basic NMR resonance assignment is a prerequisite for the validation of a heterologuous protein interaction with ACP in H.pylori. Here, the results of the backbone $^1H$, $^{15}N$, and $^{l3}C$ resonance assignments of the H. pylori ACP are reported using double- and triple-resonance techniques. About 97% of all of the $^1HN$, $^{15}N$, $^{13}CO$, $^{13}C{\alpha}$, and $^{13}C{\beta}$ resonances that cover 76 of the 78 non-proline residues are clarified through sequential- and specific-assignments. In addition, four helical regions were clearly identified on the basis of the resonance assignments.

• BMB Reports
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• 제38권5호
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• pp.591-594
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• 2005

One of the small proteins from Helicobacter pylori, HP1242, was investigated by the solution nuclear magnetic resonance (NMR) spectroscopy. HP1242 is known as a 76-residue conserved hypothetical protein and its function cannot be identified based on sequence homology. Here, the results of the backbone $^1H$, $^{15}N$, and $^{13}C$ resonance assignments of the HP1242 are reported using double- and triple-resonance techniques. About 95% of all of the $^1HN$, $^{15}N$, $^{13}CO$, $^{13}C{\alpha}$, and $^{13}C{\beta}$ resonances that cover 75 non- Proline residues of the 76 residues are clarified through sequential- and specific- assignments. In addition, three helical regions were clearly identified on the basis of the resonance assignments.

• 한국자기공명학회논문지
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• 제19권1호
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• pp.49-53
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• 2015

MRA1997 is a 76-residue conserved hypothetical protein of Mycobacterium tuberculosis H37Ra, one of the most pathogenic bacterial species and the causative agent of tuberculosis. In this study, the sequence-specific backbone resonance assignment of MRA1997 was performed using NMR spectroscopy. Approximately 88.3% of the total resonances could be unambiguously assigned. By analyzing deviations of the $C{\alpha}$ and $C{\beta}$ chemical shift values, the secondary structure of MRA1997 was calculated. The result revealed that secondary structure of MRA 1997 consists of one ${\alpha}$-helix and five ${\beta}$-sheets. Our structural study will be a footstone towards the characterization of the three-dimensional structure of MRA1997.

• 한국자기공명학회논문지
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• 제17권2호
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• pp.105-110
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• 2013

HP1492 is a NifU-like protein of Helicobacter pylori (H. pylori) and plays a role as a scaffold which transfer Fe-S cluster to Fe-S proteins like Ferredoxin. To understand how to bind to iron ion or iron-sulfur cluster, HP1492 was expressed and purified in Escherichia coli (E. coli). From the NMR measurement, we could carry out the sequence specific backbone resonance assignment of HP1492. Approximately 91% of all resonances could be assigned unambiguously. By analyzing results of CSI and TALOS from NMR data, we could predict the secondary structure of HP1492, which consists of three ${\alpha}$-helices and three ${\beta}$-sheets. This study is an essential step towards the structural characterization of HP1492.