• Journal of the Korean Magnetic Resonance Society
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• v.20 no.4
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• pp.138-142
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• 2016

Replication Protein A (RPA) is the eukaryotic single-stranded DNA binding protein. It involves in DNA replication, repair, and damage response. Among three subunits, RPA70 has a protein-protein binding domain (RPA70N) at the N-terminal. It has known that the domain recruits several damage response proteins to the damaged site. Also, it is suggested that there are more candidates that interact with RPA70N. Even though several studies performed on the structural aspects of RPA70N and its ligand binding, the backbone assignments of RPA70N is not available in public. In this study, we present the backbone assignments of RPA70N.

• Journal of the Korean Chemical Society
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• v.59 no.1
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• pp.31-35
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• 2015

Diastereoselective reduction of 2,3-dioxo-4-carboxy-5-(substituted)pyrrolidine 1 by $NaBH_4/AcOH$ and heterogenous hydrogenation were reported. Stereochemical assignment and diastereomeric ratios of the products were determined using $^1H$ NMR and single crystal X-ray analyses. The steric factors of the C-5 substituents of the pyrrolidinone was shown to have an interesting influence on both the yield and diastereoselectivity of the reduced product.

• Journal of the Korean Magnetic Resonance Society
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• v.10 no.2
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• pp.155-162
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• 2006

Angiogenin is unique among angiogenic molecules in that it is a member of the pancreatic ribonuclease superfamily and, in fact, is a ribonucleolytic enzyme. Its enzymatic activity is extremely weak compared to that of the digestive RNases but is critical for its capacity to induce neovascularization. In this study, we completed the backbone resonance assignment of bovine angiogenin using triple resonance NMR experiments of $^{15}N\;and/or\;^{13}C$ isotope labeled protein and investigated the chemical shift variation upon binding with inhibitor phosphate ion and determine the phosphate binding site.

• Natural Product Sciences
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• v.26 no.4
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• pp.283-288
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• 2020

Microbial transformation of a potent progestin, norethisterone (17��-hydroxy-19-nor-17α-pregn-4-en-20-yn-3-one) (1) was carried out by using two filamentous fungi Aspergillus niger and Penicillium citrinum. Biotransformation of 1 with A. niger yielded a hydroxylated transformed product 10��,17��-diydroxy-19-nor-17α-pregn-4-en-20-yn-3-one (2) whereas 11��,17��-diydroxy-19-nor-17α-pregn-4-en-20-yn-3-one (3) was obtained through microbial transformation of 1 by P. citrinum. It is the first report of their production from 1 by using A. niger and P. citrinum with complete 1H- and 13C-NMR assignment. The structures of both metabolites were characterized by various spectroscopic techniques and reported data.

• Journal of the Korean Chemical Society
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• v.39 no.7
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• pp.559-563
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• 1995

The three metabolites, Germacrene alcohol(1), Aaptamine(2) and Hexacyclic terpene(3) were isolated from Marine Sponge Luffariella sp., collected in October 1992, Manado Bay, Sulawesi in Indonesia showed in vitro activity against KB cancer cell line, and structure assignment for 1 was corrected by comparison of their spectral data with the literature $values^1$. Their structure were elucidated by $^1H$, $^13C$ NMR, $^1H$ $^13C$(1 bond) Heteronuclear Multiple Quantum Coherence Spectroscopy$(HMQC)^2$, $^1H$ $^13C$(2 and 3 bond) Heteronuclear Multiple Bond Correlation Spectroscopy$(HMBC)^3$, Electron Impact Mass Spectroscopy(EI ms), Ultra-violet Spectroscopy(UV) and Infrared Spectroscopy(IR).

• Molecules and Cells
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• v.24 no.3
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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.

• Korean Journal of Pharmacognosy
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• v.27 no.1
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• pp.26-31
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• 1996

A sesquiterpene ortho-naphtpoquinone was isolated from the 80% aqueous methanolic extract of root bark of Ulmus davidiana Planch whose stem and root bark have been used as an oriental medicine for the treatment of edema, mastitis, gastric cancer and inflammation. On the basis of spectral data obtained from UV-vis, IR, HR-EIMS and NMR spectrometry, including the pulse field gradient (PFG) HMQC and HMBC techniques, the structure of this compound was determined as 2,3-dihydro-3-hydroxy-3,6,9-trimethylnaphtho(1,8-b,c)pyran-7,8-dione which has been known as mansonone 1. This compound has been isolated only from the heart-wood of Mansonia altissima Chev, a Sterculiacea from West Africa. Thus, this compound was isolated for the second time from natural source in this study. This is the first report to present the carbon chemical shift assignment of mansonone I.

• Molecules and Cells
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• v.20 no.3
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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.

• Biotechnology and Bioprocess Engineering:BBE
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• v.9 no.3
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• pp.212-216
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• 2004

Peroxynitrite formation in vivo is implicated in numerous human diseases and there is considerable interest in the use of antioxidants and natural products for their treatment. The three components (1-3) isolated from Sargassum thunbergii as well as the organic solvent-soluble fractions and the aqueous layer of S. thunbergii were evaluated for their potential to scavenge authentic ONOO$\^$-/ and ONOO$\^$-/ derived from 3-morpholinosydnonimine (SIN-1). The antioxidant activity of the individual fractions was in the order of 85% aqueous (aq.) MeOH＞n$\^$-/ BuOH＞n-hexane＞H$_2$O. The three known compounds, sargahydroquinoic acid (1), sargaquinoic acid (2) and sargachromenol (3) showed peroxynitrite-scavenging activities comparable to those of L-ascorbic acid and penicillamine. These results showed a possible antioxidant activity in major constituents of S. thunbergii.

• Bulletin of the Korean Chemical Society
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• v.20 no.3
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• pp.291-296
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• 1999

The immobilization of APTMS(3-(2-aminoethylamino)propyltrimethoxysilane) and AAPTMS(3-(2-(2-aminoethyl)aminoethylanino)propyltrimethoxysilane) on the surface of high quality mesoporous molecular sieves MCM-41 and MCM-48 have been confirmed by F.T.-IR spectroscopy, Raman spectroscopy, 29Si solid state NMR, and a surface polarity measurement using Reichardt's dye. The formation of metal (Co(Ⅱ), Ni(Ⅱ), and Cu(Ⅱ)) complexes by immobilized aminosilanes have been investigated by photoacoustic spectroscopy(PAS). The assignment of UV-Vis. PAS bands makes it possible to identify the structure of metal complexes within mesoporous molecular sieves. Co(Ⅱ) ion may be coordinated mainly in a tetrahedral symmetry by two APTMS onto MCM-41, and in an octahedral one by two AAPTMS. Both Ni(Ⅱ) and Cu(Ⅱ) coordinated by aminosilanes within MCM-41 form possibly the octahedral complexes such as [Ni(APTMS)2(H20)2]2+, [Ni(AAPTMS)2]2+, [Cu(APTMS)2(H2O)2]2+, and [Cu(AAPTMS)(H2O)3]2+, respectively. The PAS band shapes of complexes onto MCM-48 are similar to those of corresponding MCM-41 with the variation of PAS intensity. Most of metal ion(Ⅱ) within MCM-41 and MCM-48 are coordinated by aminosilanes without the impregnation on the surface.