• Journal of the Korean Magnetic Resonance Society
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• v.18 no.2
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• pp.63-68
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• 2014

$^7Li$ nuclear magnetic resonance (NMR) spectra have been observed for $LiMPO_4$ (M = Fe, Mn) samples, as a promising cathode material of lithium ion battery. Observed $^7Li$ shifts of $LiFe_{1-x}Mn_xPO_4$ (x = 0, 0.6, 0.8, and 1) synthesized with solid-state reaction are compared with calculated $^7Li$ shift ranges based on the supertranferred hyperfine interaction of Li-O-M. Ex situ $^7Li$ NMR study of $LiFe_{0.4}Mn_{0.6}PO_4$ in different cut-off voltage for the first charge process is also performed to understand the relationship between $^7Li$ chemical shift and oxidation state of metals affected by delithiation process. The increment of oxidation state for metals makes to downfield shift of $^7Li$ by influencing the supertranferred hyperfine interaction.

• Journal of Biosystems Engineering
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• v.28 no.3
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• pp.261-268
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• 2003

Ten MHz pulsed NMR spectrometer was used to measure the magnetic resonance characteristics of Korean red ginseng. The difference in the internal structures of good and bad red ginsengs was examined by their NMR characteristics. Average values of $T_1$ and free induction decay(FID) ratios of under grade Korean red ginseng were the highest among the three groups categorized as normal, medium and under grades Korean red ginseng and average values of $T_2$ and $T_2$$^{＊}$ of them were the lowest among the three groups. Principal component analysis(PCA) was used to observe the contribution of measured NMR values to the grade of Korean red ginseng. The measured $T_1$, $T_2$, $T_2$$^{＊}$ and FID ratio of 79 Korean red ginsengs classified as normal grade, medium grade and under grade were examined using PCA analysis. Cumulative variance of PC1 through PC3 occupied more than 90% of total variance at first and second NMR measurement. Plots of PC scores for the most important PCs showed that normal red ginseng samples were distributed around the left region of PC1 axis and most of the undergrade red ginseng samples were scattered around the right region of PC1 axis.

• Journal of the Korean Magnetic Resonance Society
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• v.20 no.4
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• pp.102-108
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• 2016

With the rapid increase of data on protein-protein interactions, the need for delineating the 3D structures of huge protein complexes has increased. The protocols for determining nuclear magnetic resonance (NMR) structure can be applied to modeling complex structures coupled with sparse experimental restraints. In this report, I suggest the use of multiple rigid bodies for improving the efficiency of NMR-assisted structure modeling of huge complexes using CYANA. By preparing a region of known structure as a new type of residue that has no torsion angle, one can facilitate the search of the conformational spaces. This method has a distinct advantage over the rigidification of a region with synthetic distance restraints, particularly for the calculation of huge molecules. I have demonstrated the idea with calculations of decaubiquitins that are linked via Lys6, Lys11, Lys27, Lys29, Lys33, Lys48, or Lys63, or head to tail. Here, the ubiquitin region consisting of residues 1-70 was treated as a rigid body with a new residue. The efficiency of the calculation was further demonstrated in Lys48-linked decaubiquitin with ambiguous distance restraints. The approach can be readily extended to either protein-protein complexes or large proteins consisting of several domains.

• Journal of the Korean Magnetic Resonance Society
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• v.16 no.1
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• pp.46-66
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• 2012

Metabolomic studies using human urine have shown that human metabolism is altered by a variety of environmental, cultural, and physiological factors. Comprehensive information about normal human metabolite profiles is necessary for accurate clinical diagnosis of disease and for disease prevention and treatment. In this study, metabolite correlation analyses, using $^1H$ nuclear magnetic resonance (NMR) spectroscopy coupled with multivariate statistics, were performed on human urine to compare metabolic differences based on gender and/or obesity in healthy human subjects. First, we applied partial least squares discriminant analysis to the NMR spectral data set to verify the data's ability to discriminate by gender and obesity. Then, the differences in metabolite-metabolite correlation between male and female, and between normal and high body mass index (obese) subjects were investigated through pairwise correlations. Creatine and several metabolites, including isoleucine, trans-aconitate, and trimethylamine N-oxide (TMAO), exhibited different quantitative relationships depending on gender. Dimethylamine had a different correlation with glycine and TMAO, based on gender. The correlation of TMAO with amino acids was considerably lower in obese, compared to normal, subjects. We expect that the results will shed light on the metabolic pathways of healthy humans and will assist in the accurate diagnosis of human disease.

• Journal of the Korean Magnetic Resonance Society
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• v.28 no.2
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• pp.6-9
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• 2024

HscA is a Hsp70-type chaperone protein that plays an essential role to mediate the iron-sulfur (Fe-S) cluster biogenesis mechanism in Escherichia coli. Like other Hsp70 chaperones, HscA is composed of two domains: the nucleotide binding domain (NBD), which can hydrolyze ATP and use its chemical energy to facilitate the Fe-S cluster transfer process, and the substrate binding domain (SBD), which directly interacts with the substrate, IscU, the scaffold protein of an Fe-S cluster. In the present work, we prepared the isolated SBD construct of HscA (HscA(SBD)) and conducted the solution-state nuclear magnetic resonance (NMR) experiments to have its backbone chemical shift assignment information. Due to low spectral quality of HscA(SBD), we obtained all the NMR data from the sample containing the peptide LPPVKIHC, the HscA-interaction motif of IscU, from which the chemical shift assignment could be done successfully. We expect that this information provides an important basis to execute detailed structural characterization of HscA and appreciate its interaction with IscU.

• Journal of the Korean Magnetic Resonance Society
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• v.15 no.1
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• pp.40-53
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• 2011

The NMR spectra of $Li_3Rb(SO_4)_2$ crystals and their relaxation processes were investigated by using $^7Li$ and $^{87}Rb$ NMR. The relaxation rates of the $^7Li$ and $^{87}Rb$ nuclei in the crystals were found to increase with increasing temperature, and can be described by the relation $T_1^{-1}{\propto}AT^2$. The dominant relaxation mechanism for these nuclei with electric quadrupole moments is provided by the coupling of these moments to the thermal fluctuations of the local electric field gradient via Raman spin-phonon processes.

• Journal of the Korean Magnetic Resonance Society
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• v.14 no.1
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• pp.18-27
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• 2010

The NMR spectrum and spin-lattice relaxation times, $T_1$, of the $^{1}H$ nuclei in $(NH_{4})_{2}Cd_{2}(SO_{4})_{3}$ single crystals were obtained. The two minima in $T_1$ in the paraelectric phase are attributed to the reorientational motions of the $NH_{4}^{+}$ groups. The $^{1}H\;T_1$ of the $(NH_{4})_{2}Cd_{2}(SO_{4})_{3}$ crystals can be described with Bloembergen- Purcell-Pound (BPP) theory. The experimental value of $T_1$ can be expressed in terms of an isotropic correlation time ${\tau}_H$ for molecular motions by using the BPP theory, and determine the role of protons in these processes.

• Journal of the Korean Magnetic Resonance Society
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• v.13 no.1
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• pp.56-63
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• 2009

SWIRM domain, a core domain of SRG3 is well conserved in SW13, RSC8, and MOIRA family proteins. To understand structural basis for cellular functions of the SWIRM domain, we have initiated biochemical and structural studies on SWIRM domain and mutants using gelfiltration chromatography, circular dichroism and NMR spectroscopy. The structural properties of the mutant SWIRM domains (K34A and M75A) have been characterized, showing that the structures of both wild-type and mutant proteins are a-helical conformation. The data conclude that mutations at interaction sites of its binding partner protein do not affect its secondary and tertiary structure.

• Journal of the Korean Magnetic Resonance Society
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• v.20 no.3
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• pp.66-70
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• 2016

The replication protein A (RPA), is a heterotrimer with 70, 32 and 14 kDa subunits and plays a crucial role in DNA replication, recombination, and repair. The largest subunit, RPA70, binds to single-stranded DNA (ssDNA) and mediates interactions with many cellular and viral proteins. In this study, we performed nuclear magnetic resonance experiments on the complex of the DNA binding domain A of human RPA70 (RPA70A) with ssDNA, d(CCCCC), at various temperatures, to understand the temperature dependency of ssDNA binding affinity of RPA70A. Essential residues for ssDNA binding were conserved while less essential parts were changed with the temperature. Our results provide valuable insights into the molecular mechanism of the ssDNA binding of human RPA.

• Journal of the Korean Magnetic Resonance Society
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• v.22 no.4
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• pp.76-81
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• 2018

Investigation of the protein-protein interaction mode at atomic resolution is essential for understanding on the underlying functional mechanisms of proteins as well as for discovering druggable compounds blocking deleteriou interprotein interactions. Solution NMR spectroscopy provides accurate and precise information on intermolecular interactions even for weak and transient interactions, and it is also markedly useful for examining the change in the conformation and dynamics of target proteins upon binding events. In this mini-review, we comprehensively describe three unique and powerful methods of solution NMR spectroscopy, paramagnetic relaxation enhancement (PRE), pseudo-contact shift (PCS), and residual dipolar coupling (RDC), for the study on protein-protein interactions.