• Journal of the Korean Magnetic Resonance Society
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• v.20 no.3
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• pp.76-81
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• 2016

Copper is an elemental ion in living organisms. CopP from Helicobacter Pylori (HpCopP) is a copper(I)-binding protein and was suggested as regulator of copper metabolism in vivo. Previously, the metal binding property of HpCopP for Ag(I), Cu(I), and Cu(II) as well as the tertiary structure of HpCopP was shown. In this study, the dynamic profiles of HpCopP depending on metal binding were studied using ${^1H}-^{15}N$ steady-state NOE analysis. The heteroNOE experiment was performed for apo-CopP or metal-bound CopP. The obtained NOE values were analyzed and compared to figure out the effect of metals on the structural flexibility of HpCopP. As a result, Ag(I) and Cu(I) ions improved the rigidity of the structure while Cu(II) ion increased the flexibility of the structure, suggesting the oxidation of the CXXC motif decreases the structural stability of HpCopP.

• 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.

• BMB Reports
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• v.34 no.2
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• pp.95-101
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• 2001

Tissue transglutaminase (TGII, $G{\alpha}h$) belongs to a family of enzymes which catalyze post-translational modification of proteins by forming isopeptides via $Ca^{2+}$-dependent reaction. Although TGII-mediated formation of isopeptides has been implicated to play a role in a variety of cellular processes, the physiological function of TGII remains unclear. In addition to this Tease activity, TGII is a guanosine triphosphatase (GTPase) which binds and hydrolyzes GTP It is now well recognized that the GTPase action of TGII regulates a receptor-mediated transmembrane signaling, functioning as a signal transducer of the receptor. This TGII function signifies that TGII is a new class of GTP-binding regulatory protein (G-protein) that differs from "Classical" heterotrimeric G-proteins. Regulation of enzyme is an important biological process for maintaining cell integrity. This review summarizes the recent development in regulation of TGII that may help for the better understanding of this unique enzyme. Since activation and inactivation of GTPase of TGII are similar to the heterotrimeric G-proteins, the regulation of heterotrimeric G-protein in the transmembrane signaling is also discussed.

• Journal of the Korean Institute of Telematics and Electronics
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• v.25 no.1
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• pp.27-32
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• 1988

Electron Spectroscopy for Chemical Analysis(ESCA) allowes the determination of the elemental composition and the bonding state of the surface atomes in the interface between two materials. In the binding energies of ESCA spectrum, there are zero error, voltage scaling error and random error. Accurate analysis of the intensity energy response functions and accurate calibration of the energy scale are essential to use X-ray photoelectron spectron meter. At the results of the calibration of the ESCA spectra in the copper and cordierite (Mg2Al4Si5kO18) interfaces, the errors relative to the copper are -3.03 eV for the zero error -z,-197 ppm for the voltage scaling error -V and 6.9 meV for the random error -R. The method of the calibration is able to apply for the binding energy calibration of the another ESCA spectra.

• Bulletin of the Korean Chemical Society
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• v.35 no.7
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• pp.2009-2012
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• 2014

An anionic surfactant, sodium dodecylbenzene sulfonate (SDBS), was introduced during the ultrasonication process for exfoliation of graphene. The surfactant plays the roles of exfoliator and stabilizer by binding to the graphene surface. The obtained modified graphene was characterized by Fourier-transform infrared spectroscopy (FT-IR) and solid state $^{13}C$ CP/MAS NMR to analyze the binding between molecules, and by X-ray diffraction (XRD) to characterize the bulk structure. The resulting graphene exhibited good dispersion stability in both water and organic solvents.

• Journal of the Korean Applied Science and Technology
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• v.24 no.4
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• pp.362-368
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• 2007

To study the relationship between elementary biochemical states and structural states of the actomyosin crossbridges in muscle, the effects of binding of MgADP to myosin heads in the rigor muscle were examined by X-ray diffraction using synchrotron radiation. X-ray diffraction studies have been made to investigate the effects of binding of ADP on the structure of glycerinated rabbit skeletal muscle in the rigor state. The intensity increase was accompanied by a slight but distinct decrease in the 5.9 am layer-line intensity close to the meridian. These results strongly suggest that myosin heads altered their attached conformation in the proximal end toward the plane perpendicular to the fiber axis when MgADP was bound to them. We found that the intensity of the 14.5 nm-based meridional reflections increase by 20-50% when MgADP was added to the rigor muscle in the presence of hexokinase and myokinase inhibitor.

• Bulletin of the Korean Chemical Society
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• v.28 no.2
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• pp.241-245
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• 2007

The electronic structures of the new organic conducting salts, the β'- and β''-phases of (BEDT-TTF)2[(IBr2)0.2(BrICl)0.1(ICl2)0.7], were examined by calculating their electronic band structures, Fermi surfaces and HOMO-HOMO interaction energies using the extended Huckel tight binding method. On the basis of these calculations, we probed why the β'-phase is semiconducting while the β ''-phase is metallic.

• Korean Journal of Agricultural Science
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• v.38 no.4
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• pp.711-716
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• 2011

Casein micelles are the basic building block of rennet-induced gels. The stiffness of these gels is increased with reaction time. This is probably due to the continuous participation of activated casein micelles into growing network. Dual binding model of casein micelles, which explains assembly of casein and colloidal calcium phosphate, can provides fairly reasonable explanation for the changes in mechanical properties of rennet-induced gels made from different milk pHs and varying colloidal calcium phosphates. The changes in stiffness of these gels would be used for controlling textural properties of cheeses.

• YAKHAK HOEJI
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• v.31 no.5
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• pp.322-329
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• 1987

A rapid and sensitive spectrophotometric method has been developed for quantitation of some phenothiazine derivatives (PTZDS). The method depends on the formation of insoluble yellow complexes between PTZDS and picric acid (PCA) in aqueous layer. These complexes are quantitatively extracted from aqueous phase into chloroform. The binding ratio of PTZDS-PCA complexes were presumed as PTZDS-1 to PCA-1 by means of mole ratio and continuous variation methods. The complexes are stable for more than 24hours in chloroform layer at room temperature. Most of compounds associated with pharmaceutical preparation of PTZDS do not interfere with this method. However, chlorpheniramine and diphenhydramine interfere with the riaethod. The binding state of PTZDS-PCA complexes were presumed by IR and $^1$H-NMR spectra as intermolecular hydrogen bonding.

• Bulletin of the Korean Chemical Society
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• v.3 no.3
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• pp.122-129
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• 1982

In order to extend our understanding on the multiple inhibition enzyme kinetics, a general equation of an enzyme reaction in the presence of two different reversible inhibitors was derived by what we call "match-box mechanism" under the combined assumption of steady-state and quasi-equilibrium for inhibitor binding. Graphical methods were proposed to analyze the multiple inhibition of an enzyme by any given sets of different inhibitors, i.e., competitive, noncompetitive, and uncompetitive inhibitors. This method not only gives an interaction factor $({\alpha})$ between two inhibitors, but also discerns ${\alpha}_1$ and ${\alpha}_2$ with and without substrate binding, respectively. The factors involved in the dissociation constants of inhibitors can also be evaluated by the present plot. It is also shown that the present kinetic approach can be extended to other forms of activators or hydrogen ions with some modification.