• Bulletin of the Korean Chemical Society
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• v.32 no.10
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• pp.3702-3706
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• 2011

The conformation of a neuropeptide, substance P (SP), in isotropic (q = 0.5) acidic bicelles was investigated using two-dimensional NMR techniques. By the nuclear Overhauser effect (NOE) cross peaks between SP and long-chain lipid molecules SP was probed to bind on the flat surface of the disc-like bicelles. Structural analysis of NMR data indicated that the helical conformation of SP extended to the C-terminal region of Leu10 as well as in the mid-region from Pro4 to Phe8. As compared with the conformations of SP bound on the sodium dodecylsulfate (SDS) or the dodecylphosphocholine (DPC) micelles with curved surfaces, the surface curvature of the membrane mimics was found to be one of the major factors inducing the biologically relevant conformation of SP. The negative surface charge of the membrane is also a key factor inducing both the binding of SP on the membrane and its biologically active structure.

• YAKHAK HOEJI
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• v.44 no.2
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• pp.115-118
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• 2000

From the MeOH extract of Bombycis corpus inoculated by Beauberia bassiana 101A, two cyclodepsipeptides, bassianolide (1) and beaubericin (2), were isolated and their structures were determined by one and two dimensional NMR studies. Compounds 1 and 2 exhibited cytotoxicity against cultured human tumor cell lines.

• Journal of the Korean Magnetic Resonance Society
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• v.13 no.1
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• pp.7-14
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• 2009

The spectral data were collected from the two 600 MHz spectrometers from the two major manufacturers, Broker and Varian. The samples were prepared to create standard curves for quantitative measurements of metabolite concentrations. Instead of employing one-dimensional $^1H$ experiments, the two-dimensional $^1H-^{13}C$ HSQC experiments were performed for better separation of resonances. For some resonances, the high salt condition hindered the linear correlation between the intensity and actual metabolite concentration. Excluding overlapped ones, most resonances showed good linearity. Although the Varian spectrometer showed better linearity, both spectrometers were able to generate acceptable standard curves. From this data, we could identify resonances that could be used to better quantify the concentrations of the particular metabolites. With these standard curves, the quantitative measurements of the metabolites from the real samples will be facilitated.

• Proceedings of the Korean Biophysical Society Conference
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• 2003.06a
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• pp.69-69
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• 2003

Human CD99 is a ubiquitous 32-kDa transmembrane protein encoded by the mic2 gene. The major cellular functions of CD99 protein are related to homotypic cell adhension, apoptosis, vesicular protein transport, and differentiation of thymocytes or T cells. Recently it has been reported that expression of a splice variant of CD99 transmembrane protein (Type I and Type II) increases invasive ability of human breast cancer cells. To understand structural basis for cellular functions of CD99 (Type I), we have initiated studies on hCD99$^{TMcytoI}$ and hCD99$^{cytoI}$ using circular dichroism (CD) and multi-dimensional NMR spectroscopy. CD spectrum of hCD99$^{TMcytoI}$ in the presence of 200mM DPC and CHAPS displayed an existence $\alpha$-helical conformation. The solution structure of hCD99$^{cytoI}$ determined by NMR is composed of one N-terminal $\alpha$-helix, $\alpha$A, two C-terminal short $\alpha$-helix segments, $\alpha$B and $\alpha$C. While $\alpha$A and $\alpha$B are connected by the long flexible loop, $\alpha$B and $\alpha$C connected by type III$\beta$-turn. Although it has been rarely figured out the correlation between structure and functional mechanism of hCD99$^{TMcytoI}$ and hCD99$^{cytoI}$, there is possibility of dimerization or oligomerization. In addition, the feasible mechanism of hCD99$^{cytoI}$ is that it could have intramolecular interaction between the N- and C- terminal domain through large flexible AB loop.

• Journal of the Korean Wood Science and Technology
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• v.37 no.1
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• pp.73-77
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• 2009

This study was carried out to investigate the valuable antioxidative compound from extracts of Alnus hirsuta Turcz. which has a nationwide distribution. The bark (2 kg) was extracted with 70% aqueous acetone and fractionated, and the ethyl acetate and $H_2O$ fractions, separately, were chromatographed on a Sephadex LH-20 column to purify the mixture and to give two diarylheptanoid compounds. The isolated compounds were analyzed by NMR spectroscopy, including $^1H$, $^{13}C$ and two-dimensional NMR, and identified as oregonin (1) and 1,7-bis-(3,4-dihydroxyphenyl)-heptane-5-O-${\beta}$-D-xylopyranoside (2). The antioxidative activity was evaluated by DPPH method using two diarylheptanoids and acid-hydrolyzed oregonin derivative which indicated higher activity potential. Of those the acid-hydrolyzed oregonin derivative showed highly active potential with the value of 2.6 of $IC_{50}$.

• Bulletin of the Korean Chemical Society
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• v.25 no.2
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• pp.216-220
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• 2004

${\beta}$-CD and CM- ${\beta}$-CD as chiral NMR shift agents were used to resolve the enantiomers of noradrenaline (NA). The stoichiometry of each complex formed between the CDs and the enantiomers of NA was found to be 1 : 1 through the continuous variation plots. The binding constants (K) of the complexes were determined from $^1H$ NMR titration curves. This result indicated that both ${\beta}$-CD and CM- ${\beta}$-CD formed the complexes with the S(+)-NA more preferentially than its R(-)-enantiomer. The K values for the complexes with ${\beta}$-CD ($K_{S(+)}$ = 537 $M^{-1}$ and $K_{R(-)}$ = 516 $M^{-1}$ was larger than those with CM- ${\beta}$-CD ($K_{S(+)}$ = 435 $M^{-1}$ and $K_{R(-)}$ = 313 $M^{-1}$), however, enantioselectivity (${\alpha}$) of S(+)- and R(-)-NA to CM- ${\beta}$-CD ( ${\alpha}$ = 1.38) was larger than that to ${\beta}$-CD ( ${\alpha}$ = 1.04), indicating that CM- ${\beta}$-CD was the better chiral NMR solvating agents for the recognition of the enantiomers of NA. Two dimensional rotating frame nuclear Overhauser enhancement spectroscopy (ROESY) experiments were also performed to explain the binding properties in terms of spatial fitting of the NA molecule into the macrocyclic cavities.

• BMB Reports
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• v.37 no.1
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• pp.28-34
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• 2004

The discovery of biochemical and cellular functions of unannotated gene products begins with a database search of proteins with structure/sequence homologues based on known genes. Very recently, a number of frontier groups in structural biology proposed a new paradigm to predict biological functions of an unknown protein on the basis of its three-dimensional structure on a genomic scale. Structural proteomics (genomics), a research area for structure-based functional discovery, aims to complete the protein-folding universe of all gene products in a cell. It would lead us to a complete understanding of a living organism from protein structure. Two major complementary experimental techniques, X-ray crystallography and NMR spectroscopy, combined with recently developed high throughput methods have played a central role in structural proteomics research; however, an integration of these methodologies together with comparative modeling and electron microscopy would speed up the goal for completing a full dictionary of protein folding space in the near future.

• Korean Journal of Pharmacognosy
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• v.27 no.3
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• pp.207-211
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• 1996

Cumambrin A has been isolated from the dried flowers of Chrysanthemum boreale Makino. The complete $^1H$ and $^{13}C$ NMR assignment of cumambrin A was achieved from two-dimensional $^1H$-$^1H$ COSY and $^{13}C$-$^1H$ COSY spectra with the aid of homonuclear and heteronuclear double resonance experiments. The its structure has been verified by single crystal X-ray diffraction.

• Proceedings of the Korean Biophysical Society Conference
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• 1996.07a
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• pp.11-11
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• 1996

The three-dimensional structure of the carboxyl-terminal domain of the E.coli RNA polymerase $\alpha$ subunit, which is regarded as the contact site for transcription activator proteins and the promoter UP element, was determined by NMR spectroscopy. Its compact structure of four helices and two long arms enclosing its hydrophobic core shows a folding topology distinct from those of other DNA-binding proteins. (omitted)

• Proceedings of the Korean Biophysical Society Conference
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• 1996.07a
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• pp.10-10
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• 1996

High-resolution solution conformation of a novel conotoxin, [Pro 7,13] $\alpha$A-conotoxin $P_{IVA}$, GCCGSYPNAACHPCSCKDROSYCGQ-N $H_2$, has been determined by two-dimensional $^1$H nmr methods in combination with distance geometry calculation to rmsd values of 0.90 $\AA$ and 1.16 $\AA$ for the backbone and heavy atoms, respectively. Total of 324 NOE-derived interproton distance restraints including 33 long-range NOE restraints a well as 11 $\Phi$ and 7 $\chi$$^1$ torsion angle restraints were used for computation of structures. (omitted)d)