• Title/Summary/Keyword: High-resolution NMR

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On the Structure and the Extent of Disorder in Non-crystalline Silicates at High Pressure: 2 Dimensional Solid-state NMR Study (2차원 고상 핵자기 공명기를 이용한 비정질 규산염의 고압구조 및 무질서도에 대하여)

  • Lee Sung Keun
    • Journal of the Mineralogical Society of Korea
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    • v.18 no.1
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    • pp.45-52
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    • 2005
  • The recent development and advances in 2 dimensional solid-state NMR, particularly, triple quantum (3Q) MAS NMR yield much improved resolution compared with conventional 1 dimensional MAS NMR, allowing us to study the distributions of cations and anions in the non-crystalline silicate glasses and melts. Here, we present the recent progress made by 3QMAS NMR spectra of silicate glasses quenched from melts at pressures up to 10 GPa in a multi-anvil apparatus, revealing previously unknown details of structures of covalent oxide glasses and melts at high pressure.

Stable Isotope Labeling of Proteins in Mammalian Cells

  • Lee, KyungRyun;Lee, Jung Ho
    • Journal of the Korean Magnetic Resonance Society
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    • v.24 no.3
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    • pp.77-85
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    • 2020
  • Stable isotope enrichment in proteins is necessary for high-resolution nuclear magnetic resonance (NMR) experiments. Although methods for 13C, 15N and 2H-enrichment in prokaryotic cells are well established, full processing and correct folding of complex protein systems require higher organisms as the expression host. In the present study, we review recent efforts to enrich stable isotopes in mammalian cells for protein NMR studies.

Solid-state NMR Study on Membrane Protein Structure in Biological Condition

  • Kang, Su-Jin;Lee, Bong-Jin
    • Journal of the Korean Magnetic Resonance Society
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    • v.16 no.2
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    • pp.103-110
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    • 2012
  • Membrane proteins play a essential role in the biological systems and it is not easy to handle a membrane protein for its structural study. Solid-state NMR (ssNMR) can be a good tool to investigate the structures and dynamics of membrane proteins. In ssNMR, Magic Angle Spinning (MAS) and Cross Polarization (CP) can be utilized to reduce the line-broadening, leading to high resolution and sensitivity in the spectrum. ssNMR, if combined with other spectroscopic methods, can provide us a enough knowledge on structures and dynamics of membrane proteins in biological condition.

Determination of Water with Trifluoroacetic Anhydride by NMR (Trifluoroacetic Anhydride를 이용한 NMR에 의한 수분정량)

  • 이왕규;박만기;김박광;권세호;성방훈
    • YAKHAK HOEJI
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    • v.26 no.4
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    • pp.257-260
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    • 1982
  • Measurement of water is a subject of continued interest. High resolution proton magnetic resonance has not been very effective in the determination of water. Especially spectral overlap with other proton signals from the sample is undesirable result. However, trifluoroacetic anhydride reacts with water and forms trifluoroacetic acid and the proton signal of trifluoroacetic acid did not overlap with that of samples. By use of this fact, water in acetone, ethyl ether, dioxane, dichloroethane and methyl isobutyl ketone is analyzed by high resolution proton magnetic resonance (PMR). This method is capable of detecting as little as 200ppm of $H_{2}O$. And it is very rapid, simple and accurate.

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The High Resolution NMR Solution Structure of Monocyte Chemoattractant Protein-3

  • Kwon Do-Yoon;Lee Duck-Yeon;Sykes Brian D.;Kim Key-Sun
    • Journal of the Korean Magnetic Resonance Society
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    • v.9 no.2
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    • pp.74-92
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    • 2005
  • The high resolution solution structure of MCP-3 was determined using multinuclear, multidimensional NMR spectroscopy with an expressed and $^{13}C-\;and\;^{15}N-labeled$ protein. The MCP-3 has a typical chemokine fold including 3 anti-parallel $\beta-sheets$, and a C-terminal helix, but it exists as a monomer in solution under the conditions where the structure was determined (2 mM, pH 5.1 at $30^{\circ}C$). Based on the structure and the amino acid sequence compared to other chemokines we propose that Ile20 and Leu25 in MCP-3 play key roles in the formation of N-loop (residues between the $2^{nd}$ cysteine and the I sheet) which has been implicated as a determinant of chemokine specificity. Additional receptor binding surface is supplied by the 40s loop (residues between the 2 and the 3 sheet) and the binding interface of the acidic N-terminal region of chemokine receptor to MCP-3 would resemble the dimerization interface of CC type dimer.

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Low-ε Static Probe Development for 15N-1H Solid-state NMR Study of Membrane Proteins for an 800 MHz NB Magnet

  • Park, Tae-Joon;Choi, Sung-Sub;Jung, Ji-Ho;Park, Yu-Geun;Kim, Yongae
    • Bulletin of the Korean Chemical Society
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    • v.34 no.3
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    • pp.823-826
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    • 2013
  • A low-${\varepsilon}$ solid-state NMR(Nuclear Magnetic Resonance) probe was developed for the spectroscopic analysis of two-dimensional $^{15}N-^1H$ heteronuclear dipolar coupling in dilute membrane proteins oriented in hydrated and dielectrically lossy lipid environments. The system employed a 800 MHz narrow-bore magnet. A solenoid coil strip shield was used to reduce deleterious RF sample heating by minimizing the conservative electric fields generated by the double-tuned resonator at high magnetic fields. The probe's design, construction, and performance in solid-state NMR experiments at high magnetic fields are described here. Such high-resolution solid-state NMR spectroscopic analysis of static oriented samples in hydrated phospholipid bilayers or bicelles could aid the structural analysis of dilute biological membrane proteins.

The Development and Application of Chirotechnology Using Chiral Crown Ethers for Enantiomer Separation (광학분리를 위한 키랄 크라운 에테르를 이용한 키랄공학의 개발과 응용)

  • Paik, Man-Jeong;Yun, Won-Nam;Lee, Won-Jae
    • KSBB Journal
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    • v.27 no.4
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    • pp.199-206
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    • 2012
  • Chiral crown ethers are synthetic macrocyclic polyethers that bind protonated chiral primary amines with high selectivity and affinity. They have been widely used to separate or distinguish the enantiomers of chiral compounds containing a primary amino moiety by high-performance liquid chromatography, capillary electrophoresis, and NMR spectroscopy. In this paper, two important chiral crown ethers including chiral binaphthyl unit and (18-crown-6)-2,3,11,12-tetracarboxylic acid as chiral selectors are focused. And several chiral resolution techniques and their applications in chirotechnology using these chiral crown ethers with related chiral recognition mechanism studies are reviewed. Especially, it was shown that the commercially available HPLC columns based on (18-crown-6)-2,3,11,12-tetracarboxylic acid have been developed and successfully applied for the resolution of various primary amino compounds including amino acids.

Conformational Analysis of Catecholamines-Raman, High Resolution NMR, and Conformational Energy Calculation Study

  • Park Mi-Kyung;Yoo Hee-Soo;Kang Young Kee;Lee Nam-Soo;Ichiro Hanazaki
    • Bulletin of the Korean Chemical Society
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    • v.13 no.3
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    • pp.230-235
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    • 1992
  • The conformational analysis has been done for catecholamines (dopamine, norepinephrine, and epinephrine) in the cationic and di-anionic states. The species responsible for adsorption on silver metal surface is anionic deprotonated at hydroxyl groups of catechol moiety, i.e., di-anionic states of catecholamines. This was deduced from Fourier-transform Raman spectra of sodium salts of catecholamines. High resolution proton NMR (400 MHz) spectra of catecholamines in basic and neutral $D_2O$ solution show that the conformations of norepinephrine and epinephrine in the di-anionic states are preferred in gauche, but not for dopamine in the di-anionic state. However the energy difference between trans and gauche of catecholamines in the protonated cationic states is small enough to rotate freely through C-C bond in ethylamine moiety. The conformational calculations using an empirical potential function and the hydration shell model (a program CONBIO) show consistent with above experimental results. The calculations suggest that the species of catecholamines adsorbed on silver metal surface would be in favor of the gauche conformations.