• 대한화학회지
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• 제39권7호
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• pp.559-563
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• 1995

인도네시아 Manado만의 Sulawesi에서 채집한 KB cancer cell line에 대해 in vitro로 활성을 갖는 해면 Luffariella sp.으로부터 Germacrene alcohol(1), Aaptamine(2) 및 Hexacyclic terpene(3)을 분리하였으며, 1에대한 spectral data는 문헌치와 비교${\cdot}$분석하여 수정하였다. 이들을 $^1H$, $^13C$ NMR, $^1H$ $^13C$(bond) Heteronuclear Multiple Quantum Coherence Spectroscopy(HMQC), $^1H$$^13C$(2 and 3 bond)Heteronuclear Multiple Bond Correlation Spectroscopy(HMBC), Electron Impact Mass Spectroscopy(EI ms), UV 및 IR에 의해 밝혔다.

• 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.

• 한국자기공명학회논문지
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• 제16권2호
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• pp.172-184
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• 2012

The prokaryotic molecular chaperone Hsp33 achieves its holdase activity upon response to oxidative stress particularly at elevated temperature. Despite many structural studies of Hsp33, which were conducted mainly by X-ray crystallography, the actual structures of the Hsp33 in solution remains controversial. Thus, we have initiated NMR study of the reduced, inactive Hsp33 monomer and backbone NMR assignments were obtained in the present study. Based on a series of triple resonance spectra measured on a triply isotope-[$^2H/^{13}C/^{15}N$]-labeled protein, sequence-specific assignments of the backbone amide signals observed in the 2D-[$^1H/^{15}N$]TROSY spectrum could be completed up to more than 96%. However, even considering the small portion of non-assigned resonances due to the lack of sequential connectivity, we confirmed that the total number of observed signals was quite smaller than that expected from the number of amino acid residues in Hsp33. Thus, it is postulated that peculiar dynamic properties would be involved in the solution structure of the inactive Hsp33 monomer. We expect that the present assignment data would eventually provide the most fundamental and important data for the progressing studies on the 3-dimensional structure and molecular dynamics of Hsp33, which are critical for understanding its activation process.

• 대한화학회지
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• 제47권1호
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• pp.38-42
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• 2003

신농약 개발을 목적으로 isosterism 이론을 근거로 하여 선도화합물, 2-imino-1,3-thiazoline의 분자 수정을 통하여 분자내에 1,3-thiazole과 urea기가 포함된 새로운 화합물 2를 디자인하였다. N-Methylthiourea 5와 bromoacetonitrile을 에탄올 용액 중에서 반응시켜 위치 선택적으로 생성된 2,4-diimino-1,3-thiazole 4를 phenylisocyanate 유도체와 반응하여 화합물 2의 tautomer인 7을 얻었고 이것의 구조를 여러 가지 스펙트럼($^1H$ NMR, $^{13}C$ NMR, FT-IR, HRMS)과 X-ray 결정 데이터로부터 확인하였다. 화합물 7의 구조이성질체 8은 열역학적으로 불안정한 중간체 2,4-diimino-1,3-thiazole 6을 통하여 생성되었다.

• 한국자기공명학회논문지
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• 제17권1호
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• pp.54-58
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• 2013

SAV0506 is an 87 residue hypothetical protein from Staphylococcus aureus strain Mu50 and also predicted to have similar function to ribosome associated heat shock protein, Hsp 15. Hsp15 is thought to be involved in the repair mechanism of erroneously produced 50S ribosome subunit. In this report, we present the sequence specific backbone resonance assignment of SAV0506. About 82.5% of all resonances could be assigned unambiguously. By analyzing deviations of the $C{\alpha}$ and $C{\beta}$ chemical shift values, we could predict the secondary structure of SAV0506. This study is an essential step towards the structural characterization of SAV0506.

• 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.

• 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.

• Journal of Microbiology and Biotechnology
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• 제16권9호
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• pp.1429-1433
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• 2006

Application of recombinant protein production and particularly their isotopic enrichment has stimulated development of a range of novel multidimensional heteronuclear NMR techniques. Peptides in most cases are amenable to assignment and structure determination without the need for isotopic labeling. However, there are many cases where the availability of $^{15}N$ and/or $^{13}C$ labeled peptides is useful to study the structure of peptides with more than 30 residues and the interaction between peptides and membrane. CRAMP (Cathelicidin-Related AntiMicrobial Peptide) was identified from a cDNA clone derived from mouse femoral marrow cells as a member of cathelicidin-derived antimicrobial peptides. CRAMP was successfully expressed as a GST-fused form in E. coli and purified using affinity chromatography and reverse-phase chromatography. The yield of the CRAMP was 1.5 mg/l 1. According to CD spectra, CRAMP adopted ${\alpha}$-helical conformation in membrane-mimetic environments. Isotope labeling of CRAMP is expected to make it possible to study the structure and dynamic properties of CRAMP in various membrane systems.

• Molecules and Cells
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• 제24권3호
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• pp.437-440
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• 2007

$OGL-20P^T$-358 is a novel 66 amino acid residue protein from the hyperthermophile Thermococcus thioreducens sp. nov., strain $OGL-20P^T$, which was collected from the wall of the hydrothermal black smoker in the Rainbow Vent along the mid-Atlantic ridge. This protein, which has no detectable sequence homology with proteins or domains of known function, has a calculated pI of 4.76 and a molecular mass of 8.2 kDa. We report here the backbone $^1H$, $^{15}N$, and $^{13}C$ resonance assignments of $OGL-20P^T$-358. Assignments are 97.5% (316/324) complete. Chemical shift index was used to determine the secondary structure of the protein, which appears to consist of primarily ${\alpha}$-helical regions. This work is the foundation for future studies to determine the three-dimensional solution structure of the protein.