• 제목/요약/키워드: backbone assignment

검색결과 53건 처리시간 0.028초

통합 필터 변별도와 그래프 컬러링을 이용한 전술통신망 백본 무선 링크의 주파수 지정 방법 (Frequency Assignment Method using NFD and Graph Coloring for Backbone Wireless Links of Tactical Communications Network)

  • 함재현;박휘성;이은형;최증원
    • 한국군사과학기술학회지
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    • 제18권4호
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    • pp.441-450
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    • 2015
  • The tactical communications network has to be deployed rapidly at military operation area and support the communications between the military command systems and the weapon systems. For that, the frequency assignment is required for backbone wireless links of tactical communications network without frequency interferences. In this paper, we propose a frequency assignment method using net filter discrimination (NFD) and graph coloring to avoid frequency interferences. The proposed method presents frequency assignment problem of tactical communications network as vertex graph coloring problem of a weighted graph. And it makes frequency assignment sequences and assigns center frequencies to communication links according to the priority of communication links and graph coloring. The evaluation shows that this method can assign center frequencies to backbone communication links without frequency interferences. It also shows that the method can improve the frequency utilization in comparison with HTZ-warfare that is currently used by Korean Army.

Backbone assignment of the intrinsically disordered N-terminal region of Bloom syndrome protein

  • Min June Yang;Chin-Ju Park
    • 한국자기공명학회논문지
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    • 제27권3호
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    • pp.17-22
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    • 2023
  • Bloom syndrome protein (BLM) is a pivotal RecQ helicase necessary for genetic stability through DNA repair processes. Our investigation focuses on the N-terminal region of BLM, which has been considered as an intrinsically disordered region (IDR). This IDR plays a critical role in DNA metabolism by interacting with other proteins. In this study, we performed triple resonance experiments of BLM220-300 and presented the backbone chemical shifts. The secondary structure prediction based on chemical shifts of the backbone atoms shows the region is disordered. Our data could help further interaction studies between BLM220-300 and its binding partners using NMR.

Backbone Assignment of Phosphorylated Cytoplasmic Domain B of Mannitol Transporter IIMtl in Thermoanaerobacter Tengcongensis

  • Lee, Ko On;Suh, Jeong-Yong
    • 한국자기공명학회논문지
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    • 제21권1호
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    • pp.20-25
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    • 2017
  • The cytoplasmic domains A and B of the mannitol transporter enzyme $II^{Mtl}$ are covalently linked in Escherichia coli, but separately expressed in Thermoanaerobacter Tengcongensis. The phosphorylation of domain B ($TtIIB^{Mtl}$) substantially increases the binding affinity to the domain A ($TtIIA^{Mtl}$) in T. Tengcongensis. To understand the structural basis of the enhanced domain-domain interaction by protein phosphorylation, we obtained NMR backbone assignments of the phospho-$TtIIB^{Mtl}$ using a standard suite of triple resonance experiments. Our results will be useful to monitor chemical shift changes at the active site of phosphorylation and the binding interfaces.

Backbone assignment of the anticodon binding domain of human Glycyl-tRNA synthetase

  • Mushtaq, Ameeq Ul;Cho, Hye Young;Byun, Youngjoo;Jeon, Young Ho
    • 한국자기공명학회논문지
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    • 제20권2호
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    • pp.50-55
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    • 2016
  • Backbone $^1H$, $^{13}C$ and $^{15}N$ resonance assignments are presented for the anticodon binding domain (residues 557-674) of human glycyl-tRNA synthetase (GRS). Role of the anticodon binding domain (ABD) of GRS as an anticancer ligand has recently been reported and its role in other diseases like Charcot-Marie-Tooth (CMT) and polymyositis have increased its interest. NMR assignments were completed using the isotope [$^{13}C/^{15}N$]-enriched protein and chemical shifts based secondary structure analysis with TALOS+ demonstrate similar secondary structure as reported in X-ray structure PDB 2ZT8, except some C-terminal residues. NMR signals from the N-terminal residues 557 to 571 and 590 to 614 showed very weak or no signals exhibiting dynamics or conformational exchange in NMR timescale.

1H, 15N, and 13C backbone assignments and secondary structure of the cytoplasmic domain A of mannitol trasporter IIMannitol from Thermoanaerobacter Tencongensis phosphotransferase system

  • Lee, Ko-On;Suh, Jeong-Yong
    • 한국자기공명학회논문지
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    • 제19권1호
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    • pp.42-48
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    • 2015
  • The mannitol transporter Enzyme $II^{Mtl}$ of the bacterial phosphotransferase system has two cytoplasmic phosphoryl transfer domains $IIA^{Mtl}$ and $IIB^{Mtl}$. The two domains are linked by a flexible peptide linker in mesophilic bacterial strains, whereas they are expressed as separated domains in thermophilic strains. Here, we carried out backbone assignment of $IIA^{Mtl}$ from thermophilic Thermoanaerobacter Tencongensis using a suite of heteronuclear triple resonance NMR spectroscopy. We have completed 94% of the backbone assignment, and obtained secondary structural information based on torsion angles derived from the chemical shifts. $IIA^{Mtl}$ of Thermoanaerobacter Tencongensis is predicted to have six ${\beta}$ strands and six ${\alpha}$ helices, which is analogous to $IIA^{Mtl}$ of Escherichia coli.

Backbone NMR chemical shift assignment of transthyretin

  • Kim, Bokyung;Kim, Jin Hae
    • 한국자기공명학회논문지
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    • 제25권1호
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    • pp.8-11
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    • 2021
  • Transthyretin (TTR) is an important transporter protein for thyroxine (T4) and a holo-retinol protein in human. In its native state, TTR forms a tetrameric complex to construct the hydrophobic binding pocket for T4. On the other hand, this protein is also infamous for its amyloidogenic propensity, which causes various human diseases, such as senile systemic amyloidosis and familial amyloid polyneuropathy/cardiomyopathy. In this work, to investigate various structural features of TTR with solution-state nuclear magnetic resonance (NMR) spectroscopy, we conducted backbone NMR signal assignments. Except the N-terminal two residues and prolines, backbone 1H-15N signals of all residues were successfully assigned with additional chemical shift information of 13CO, 13Cα, and 13Cβ for most residues. The chemical shift information reported here will become an important basis for subsequent structural and functional studies of TTR.

Per-deuteration and NMR experiments for the backbone assignment of 62 kDa protein, Hsp31

  • Kim, Jihong;Choi, Dongwook;Park, Chankyu;Ryu, Kyoung-Seok
    • 한국자기공명학회논문지
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    • 제19권3호
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    • pp.112-118
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    • 2015
  • Hsp31 protein is one of the members of DJ-1 superfamily proteins and has a dimeric structure of which molecular weight (MW) is 62 kDa. The mutation of DJ-1 is closely related to early onset of Parkinson's disease. Hsp31 displays $Zn^{+2}$-binding activity and was first reported to be a holding chaperone in E. coli. Its additional glyoxalase III active has recently been characterized. Moreover, an incubation at $60^{\circ}C$ induces Hsp31 protein to form a high MW oligomer (HMW) in vitro, which accomplishes an elevated holding chaperone activity. The NMR technique is elegant method to probe any local or global structural change of a protein in responses to environmental stresses (heat, pH, and metal). Although the presence of the backbone chemical shifts (bbCSs) is a prerequisite for detailed NMR analyses of the structural changes, general HSQC-based triple resonance experiments could not be used for 62 kDa Hsp31 protein. Here, we prepared the per-deuterated Hsp31 and performed the TROSY-based triple resonance experiments for the bbCSs assignment. Here, detailed processes of per-deuteration and the NMR experiments are described for other similar NMR approaches.

Backbone assignment of HMGB1 A-box and molecular interaction with Hoxc9DBD studied by paramagnetic probe

  • Choi, Ji Woong;Park, Sung Jean
    • 한국자기공명학회논문지
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    • 제25권2호
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    • pp.17-23
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    • 2021
  • High mobility group protein B1 (HMGB1) is a highly conserved, non-histone, chromatin associated nuclear protein encoded by HMGB1 gene. HMGB1 proteins may be general co-factors in Hox-mediated transcriptional activation that facilitate the access of Hox proteins to specific DNA targets. It is unclear that the exact binding interface of Hoxc9DBD and HMGB1. To identify the interface and binding affinity of Hoxc9DBD and HMGB1 A-box, the paramagnetic probe, MTSL was used in NMR titration experiment. It is attached to the N-terminal end of HMGB1 A-box by reaction with thiol groups. The backbone assignment of HMGB1 A-box was achieved with 3D NMR techinques. The 15N-labeled HMGB1 A-box was titrated with MTSL-labeled Hoxc9DBD respectively. Based on the chemical shift changes we can identify the interacting residues and further map out the binding sites on the protein structure. The NMR titration result showed that the binding interface of HMGB1 A-box is around loop-1 between helix-1 and helix-2. In addition, the additional contacts were found in N- and C-terminus. The N-terminal arm region of Hoxc9DBD is the major binding region and the loop between helix1 and helix2 is the minor binding region.

Design and Configuration of Reconfigurable ATM Networks with Unreliable Links

  • Lee, Jong-Hyup
    • ETRI Journal
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    • 제21권4호
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    • pp.9-22
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    • 1999
  • This paper considers a problem of configuring both physical backbone and logical virtual path (VP) networks in a reconfigurable asynchronous transfer mode (ATM) network where links are subject to failures. The objective is to determine jointly the VP assignment, the capacity assignment of physical links and the bandwidth allocation of VPs, and the routing assignment of traffic demand at least cost. The network cost includes backbone link capacity expansion cost and penalty cost for not satisfying the maximum throughput of the traffic due to link failures or insufficient link capacities. The problem is formulated as a zero-one non-linear mixed integer programming problem, for which an effective solution procedure is developed by using a Lagrangean relaxation technique for finding a lower bound and a heuristic method exploited for improving the upper bound of any intermediate solution. The solution procedure is tested for its effectiveness with various numerical examples.

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Purification and Backbone Assignment of the Hypothetical Protein MTH1821 from Methanobacterium Thermoautotrophicum H

  • Kwak, Soo-Young;Lee, Woong-Hee;Shin, Joon;Ko, Sung-Geon;Lee, Weon-Tae
    • 한국자기공명학회논문지
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    • 제11권2호
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    • pp.73-84
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    • 2007
  • MTH1821 (UniProtKB/TrEMBL ID O27849) is a 96-residue hypothetical protein from the open reading frame of Methanobacterium thermoautotrophicum H one of the target organisms of structural genomics pilot project. Proteins which contain conserved sequence compared with MTH1821 have not been discovered yet and the functional and structural information for MTH1821 is not available. Here, we present the sequence-specific backbone resonance using multidimensional heteronuc1ear NMR spectroscopy and propose the secondary structure using GetSBY software. The backbone resonances of N, HN, $C_{\alpha}$, $C_{\beta}$, CO and $H_{\alpha}$ which are necessary for a prediction of secondary structure by GetSBY were assigned about 98% (557/568). The secondary structure of MTH1821 confirmed that it is comprised of four strand regions and two helical regions. This report will provide a valuable resource for the calculation solution structure of MTH1821 and for the other hypothetical protein that is targeted for structural-based functional discovery.

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