• Bulletin of the Korean Chemical Society
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• v.27 no.3
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• pp.386-388
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• 2006

Membrane proteins in highly oriented lipid bilayer samples are useful for membrane protein structure determination. We used in the past planar lipid bilayers which were aligned and supported on the glass slide. These samples were mechanically aligned in a magnetic field. However, these stacks of glass slides with planar lipid bilayers are not well suited for use with a commercial solid-state NMR probe with a round coil. Therefore, a homebuilt solid-state NMR probe was built and used with a stack of thin glass plates wherein the RF coil was wrapped directly around the flat square sample. Recently, we began to use magnetically aligned bicelles that are suitable for the structure determination of membrane proteins by solid-state NMR spectroscopy without any effort to build a flat square coil probe. These bicelle samples are well suited for use with a commercial solidstate NMR probe with a round coil, are very easy to prepare and are very stable, so that they can be kept for more than a year. In this paper, we present the solid-state NMR spectra of optimized and magnetically oriented bicelle samples of membrane proteins.

• Bulletin of the Korean Chemical Society
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• v.23 no.12
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• pp.1729-1732
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• 2002

The LB71350,(3S, 4R)-Epoxy-(5S)-[[N-(1-methylethoxy)carbonyl]-3-(methylsulfonyl)-L-valinyl]amino]-N-[2-methyl-(1R)-[(phenyl)carbonylpropyl-6-phenylhexanamide, is a novel HIV protease inhibitor. Its equilibrium solubility at room temperature was less than $40{\mu}g/mL.$ It was speculated that the low aqueous solubility might be due to the high crystalline lattice energy resulting from intermolecular hydrogen bonds. The present study was carried out to learn the solid-state characteristics of LB71350 using analytical methods such as NMR, FT-IR and XRD. $^{13}C$ Solid-state NMR, solution NMR, and FT-IR spectra of the various solid forms of LB71350 were used to identify the conformation and structure of the solid forms. The chemical shifts of $^{13}C$ solid-state NMR spectra suggest that the crystalline form might have 3 intermolecular hydrogen bondings between monomers.

• Bulletin of the Korean Chemical Society
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• v.31 no.5
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• pp.1187-1191
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• 2010

$^1H-^{15}N$ heteronuclear dipolar coupling solid-state NMR experiments on lipid bilayer or bicelle samples are very useful for the structural studies of membrane proteins. However, to study these biological samples using solid-state NMR, a specific probe with high efficiency and high capability is required. In this paper, we describe the optimized design, construction, and efficiency of a 400 MHz wide-bore $^1H-^{15}N$ solid-state NMR probe with 5-mm solenoidal rf coil for high power, multi-pulse sequence experiments, such as 2D PISEMA or 2D SAMMY.

• Journal of the Korean Magnetic Resonance Society
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• v.1 no.1
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• pp.45-58
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• 1997

Heteropoly compounds, H3PMo12O40, CsxH3-xPMo12O40, and vanadium containing heteropoly compound were characterized by Solid-state broad line 1H MAS NMR, 31P MAS NMR, and High Speed MAS 51V NMR spectroscopy of quadrupolar nuclei. The effects of calcination, dehydration, and the number of protons on the structure of heteropoly compounds were studied. The results of this study demonstrate that these Solid-state NMR techniques are very useful tools to study heteropoly compounds.

• Bulletin of the Korean Chemical Society
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• v.30 no.5
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• pp.1077-1079
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• 2009

To minimize the variance in the quantification of solid-state phases in powder samples, gently placing polycrystalline samples one next to another directly in a sample holder is better than trying to mix them homogeneously prior to transferring to a sample holder. However, the solid-state cross polarization-magic angle spinning (CP-MAS) nuclear magnetic resonance (NMR) spectroscopy results demonstrated that it is essential in this sampling method to place all the samples in the location of consistent signal sensitivity. The same sampling method may be employed in other spectroscopic quantification techniques of solid-state phases if the method to limit the sample to the location with uniform signal sensitivity in the sample holder is adapted to each technique.

• Analytical Science and Technology
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• v.17 no.5
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• pp.388-392
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• 2004

Structural studies of membrane proteins, importantly involving interpretation of genomics information, many signaling pathway and major drug target for drug discovery, are having difficulty in characterizing the function using conventional solution nmr spectroscopy and x-ray crystallography because phospholipid bilayers hindered fast tumbling and crystallization. Here, we studied the structure of the pf1 coat protein in oriented phospholipid bilayers by home-built solid-state NMR probe. Bacteriophage pf1 was purified from Paeudomonas Aeruginosa and coat protein of bacteriophage pf1 was isolated from DNA and other proteins.

• Journal of the Korean Magnetic Resonance Society
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• v.11 no.1
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• pp.42-47
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• 2007

Several hydrotalcite compounds calcined with different temperature for applications in a chlorine resistant textile were prepared, and its structural changes in dependence on the temperature were studied by using $^{27}Al$ solid-state nuclear magnetic resonance(NMR) spectroscopy. We found that the Al coordination was partly lowered from octahedral to tetrahedral site as the calcined temperature goes up. And we also investigated the hydrotalcite-treated textile for chlorine resistance by using $^{27}Al$ solid-state NMR spectroscopy.

• Proceedings of the Polymer Society of Korea Conference
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• 2006.10a
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• pp.347-347
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• 2006

Polymers containing poly(vinyl phosphonic) acid segments are promising candidates to be used as proton conducting membranes. Solid state NMR spectroscopy represents an ideal probe of proton motion on the molecular level, because it allows us to selectively detect the nuclei of interest. In this paper, we apply solid state NMR methods to poly(vinyl phosphonic) acid in order to demonstrate that the proton conduction of poly(vinyl phosphonic acid) results from P-OH proton through hydrogen bonding and that the condensation of phosphonic acid leads to decrease in proton conductivity. $^{1}H\;and\;^{31}P$ solid state NMR experiments are supported by quantum chemical computation of NMR parameters.

• Bulletin of the Korean Chemical Society
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• v.24 no.9
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• pp.1281-1283
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• 2003

Proteins in highly oriented lipid bilayer samples are useful to study membrane protein structure determination. Planar lipid bilayers aligned and supported on glass slide were prepared. These stack of glass slide with planar lipid bilayers are not well fit for commercial solid-state NMR probe with round coil. Therefore, homebuilt solid-state NMR probe was built and used for a stack of thin glass plates and RF coil is wrapping directly around the flat square sample. The overall filling factor of the coil is much better and the large surface area enhances the extent to orientation by providing uniform environments for the phospholipids and the high ratio of circumference to area reduces edge effects. $^1H\;and\;^{15}N$ double resonance probe for 400 MHz NMR (9.4T) with a flat coil (coil size: 11 mm ${\times}$ 20 mm ${\times}$ 4 mm) is constructed and tested.

• 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.