• Journal of the Korean Chemical Society
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• v.38 no.1
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• pp.21-25
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• 1994

The proton affinities of substituted imidazoles, relevant to the binding of lexitropsins that contain imidazole ring to the base pair (G-C sequence) of minor groove of DNA, are studied with the aid of EHT calculations. It is shown that proton affinity of imidazole substituted at position $\alpha$ to the basic nitrogen is slightly larger than that of imidazole substituted at N for the methylimidazole. Proton affinities of N-substituted imidazoles are found to be larger than those of imidazoles substituted at position ${\alpha}$ for a selected set of the other derivatives. As predicted the proton affinity increases when electron-donating group is attached at position N of imidazole.

• Journal of Microbiology and Biotechnology
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• v.16 no.8
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• pp.1316-1319
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• 2006

An antibody displayed phage collection (SBAE-2R), screened from a human synthetic phage antibody library (Fab 21ox), was used for the determination of dextran. The dextran-binding affinity was determined by serologically specific transmission electron microscopy (TEM) and a paper dipstick assay. The phage collection was distributed over the dextrancoated grids with 39$\pm$25 phages/$\mu$m$^2$ on the grids. Phages were not seen on dextran-coated grids exposed to the Fab 2lox phage library. The phage collection (SBAE-2R) produced 54$\pm$3 color normalized intensity (N.I.) from 125 ppm to 1,000 ppm of dextran and 5$\pm$1 (N.I.) for 63 ppm of dextran in a paper dipstick assay. This research extends the analytical options for dextran analysis by antibody displayed phage with a minimum of equipment usage.

• Proceedings of the Korean Vacuum Society Conference
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• 2010.02a
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• pp.7-8
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• 2010

The surface conductive layer (SCL) of chemical vapor deposition (CVD) diamonds has attracting much interest. However, neither photoemission electron microscopic (PEEM) nor micro-spectroscopic (PEEMS) information is available so far. Since SCL retains in an ultra-high vacuum (UHV) condition, PEEM or PEEMS study will give an insight of SCL, which is the subject of the present study. The sample was made on a Ib-type HTHP diamond (001) substrate by non-doping CVD growthin a DC-plasma deposition chamber. The SCL properties of the sample in air were; a few tens K/Sq. in sheet resistance, ${\sim}180\;cm^2/vs$ in Hall mobility, ${\sim}2{\times}10^{12}/cm^2$ in carrier concentration. The root-square-mean surface roughness (Rq) of the sample was ~0.2nm as checked by AFM. A $2{\times}1$ LEED pattern and a sheet resistance of several hundreds K/Sq. in UHV were checked in a UHV chamber with an in-situ resist-meter [1]. The sample was then installed in a commercial PEEM/S apparatus (Omicron FOCUS IS-PEEM) which was composed of electro-static-lens optics together with an electron energy-analyzer. The presence of SCL was regularly monitored by measuring resistance between two electrodes (colloidal graphite) pasted on the two ends of sample surface. Figure 1 shows two PEEM images of a same area of the sample; a) is excited with a Hg-lamp and b) with a Xe-lamp. The maximum photon energy of the Hg-lamp is ~4.9 eV which is smaller that the band gap energy ($E_G=5.5\;eV$) of diamond and the maximum photon energy of the Xe-lamp is ~6.2 eV which is larger than $E_G$. The image that appear with the Hg-lamp can be due to photo-excitation to unoccupied states of the hydrogen-terminated negative electron affinity (NEA) diamond surface [2]. Secondary electron energy distribution of the white background of Figs.1a) and b) indeed shows that the whole surface is NEA except a large black dot on the upper center. However, Figs.1a) and 1b) show several features that are qualitatively different from each other. Some of the differences are the followings: the two main dark lines A and B in Fig.1b) are not at all obvious and the white lines B and C in Fig.1b) appear to be dark lines in Fig.1a). A PEEMS analysis of secondary electron energy distribution showed that all of the features A-D have negative electron affinity with marginal differences among them. These differences can be attributed to differences in the details of energy band bending underneath the surface present in SCL [3].

• JSTS:Journal of Semiconductor Technology and Science
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• v.2 no.2
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• pp.93-101
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• 2002

We have proposed and fabricated two lateral type field emission diodes, poly-Si emitter by utilizing the local oxidation of silicon (LOCOS) and GaN emitter using metal organic chemical vapor deposition (MOCVD) process. The fabricated poly-Si diode exhibited excellent electrical characteristics such as a very low turn-on voltage of 2 V and a high emission current of $300{\;}\bu\textrm{A}/tip$ at the anode-to-cathode voltage of 25 V. These superior field emission characteristics was speculated as a result of strong surface modification inducing a quasi-negative electron affinity and the increase of emitting sites due to local sharp protrusions by an appropriate activation treatment. In respect, two kinds of procedures were proposed for the fabrication of the lateral type GaN emitter: a selective etching method with electron cyclotron resonance-reactive ion etching (ECR-RIE) or a simple selective growth by utilizing $Si_3N_4$ film as a masking layer. The fabricated device using the ECR-RIE exhibited electrical characteristics such as a turn-on voltage of 35 V for $7\bu\textrm{m}$ gap and an emission current of~580 nA/l0tips at anode-to-cathode voltage of 100 V. These new field emission characteristics of GaN tips are believed to be due to a low electron affinity as well as the shorter inter-electrode distance. Compared to lateral type GaN field emission diode using ECR-RIE, re-grown GaN emitters shows sharper shape tips and shorter inter-electrode distance.

• Journal of Microbiology and Biotechnology
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• v.2 no.4
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• pp.268-272
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• 1992

Alcohol dehydrogenase activity of Clostridium acetobutylicum ATCC 4259 was studied for its specificity against substrates in acidogenic and solventogenic cultures. The bacterium reduces propionate, valerate and caproate added to the medium to the corresponding alcohols. Acetaldehyde, propionaldehyde, butyraldhyde, pentanal, and hexanal were used as the substrates by alcohol dehydrogenase, and all were reduced to the corresponding alcohols with varying affinities and reaction velocities. Acetaldehyde showed the lowest affinity and lowest velocity while the other aldehydes showed similar $K_m\;and\;V_max$ values. NADPH was used as the electron donor for the reduction of aldehydes. Alcohol dehydrogenase activity was low in acidogenic culture, and high in solventogenic culture.

• Journal of the Korean Magnetic Resonance Society
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• v.26 no.4
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• pp.40-45
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• 2022

A small cage-like molecule (2) composed of three aminomethyl pyrroles and two hexa-substituted benzenes has been prepared by reduction of its iminopyrrole analogue (1) using NaBH₄. It was revealed by ¹H NMR spectroscopic analyses that cage molecule 2 strongly binds the fluoride anion in polar DMSO-d₆ relative to CDCl₃. Compared to that of compound 1, the lowered affinity of 2 for the fluoride anion is attributable to its increased electron density resulting from the production of thesecondary amine groups.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2005.11a
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• pp.313-314
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• 2005

Organic light emitting diodes(OLEDs) are widely used as one of the information display techniques. We synthesized (1,10-phenanthroline)- (8-hydroxyquinoline) [Zn(Phen)q]. We studied the improvement of OLEDs properties using Zn(phen)q. The Ionization Potential(IP) and the Electron Affinity(EA) of Zn(phen)q investigated using cyclic voltammetry(CV). The IP, EA and Eg were 7.leV, 3.4eV and 3.7eV, respectively. The PL spectrum of Zn(phen)q was yellowish green as the wavelength of 535nm. In this study, we used Zn(phen)q as electron transporting layer(ETL) inserted between emitting layer(EML) and cathode. As a result, Zn(phen)q is useful as electron transporting layer to enhance the performance of OLEDs.

• Archives of Plastic Surgery
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• v.35 no.1
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• pp.1-6
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• 2008

Purpose: In tissue engineering, it is important that the scaffolds have high affinity with cells for making efficient use of cells. The authors studied the binding affinity of human adipose stem cells(ASCs) to micronized acellular dermal matrix(alloderm) using biotin and avidin linkages.Methods: Human ASCs were harvested from adipose tissue obtained by abdominoplasty. ASCs($1{\times}10^4$, $5{\times}10^4$, $1{\times}10^5$, $5{\times}10^5$, $1{\times}10^6$, $5{\times}10^6$ cells) were attached to micronized alloderm(1mg) in three groups; 1) control group in which no ASCs and alloderm was treated; 2) serum group in which alloderm was exposed to fetal bovine serum; and 3) biotin group in which biotinylated cells were attached to biotinylated alloderm. The binding affinities were determined 1 day after making ASC-alloderm complexes. The proliferation rates were determined by XTT assays in 4, 7, 14, and 21 days and scanning electron microscopic examination was performed in 7 and 21 days after culture of ASC-alloderm complexes.Results: The binding affinities of the biotin group were significantly increased in all cell concentrations. Maximum binding affinity was observed at $5{\times}10^4/mg$ of micronized dermal matrix in biotin group. The viabilities were lowest in biotin group in contrast to binding affinity, but the difference was not significant. SEM showed well attachment of cells to micronized dermal matrix in all groups. Conclusion: The use of avidin/biotin facilitated human ASCs attaching to micronized acellular dermal matrix. This attachment would not disturb adipose stem cells viabilities. The present study suggests that avidin/ biotin can be used as making efficient use of cells in adipose tissue engineering.

• Proceedings of the KIEE Conference
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• 2009.07a
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• pp.1244_1245
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• 2009

Coating of amorphous nitride thin layers, such as boron nitride (BN) and carbon nitride (CN), has been performed on carbon nanotubes (CNTs) for the purpose of enhancing their electron-emission performances because those nitride films have relatively low work functions and commonly exhibit negative electron affinity behavior. The CNTs were directly grown on metal-tip (tungsten, approximately 500 nm in diameter at the summit part) substrates by inductively coupled plasma-chemical vapor deposition (ICP-CVD). Sharpening of the tungsten tips were carried out by electrochemical etching. Morphologies and microstructures of BN and CN films were analyzed by field-emission scanning electron microscopy (FE-SEM), energy dispersive x-ray (EDX) spectroscopy, and Raman spectroscopy. The electron-emission properties (such as maximum emission currents and turn-on fields) of the BN-coated and CN-coated CNT-emitters were characterized in terms of the thickness of BN and CN layers.

• BMB Reports
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• v.29 no.4
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• pp.300-307
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• 1996

ATP and ADP are potential regulators of mitochondtial respiration and at physiological concentrations they affect the rate of electron transfer between cytochrome c and cytochrome c oxidase. The electron transfer, however, depends on the electrostatic interaction between the two proteins. In order to exclude any nonspecific ionic effects by these polyvalent nucleotides, we used 2'-O-(2,4,6)trinitro(TNP)-derivatives of ATP and ADP which have three orders of magnitude higher affinity for cytochrome c oxidase. A simple titration of the fluorescence intensity of TNP by cytochrome c oxidase showed a binding stoichiometry of 2:1 cytochrome c:cytochrome c oxidase. Higher ionic strength was required for TNP-ATP than for TNP-ADP to be dissociated from cytochrome c oxidase, indicating that the negative charges on the phosphate group are at least partially responsible for the binding. In both spectrophotometric and polarographic assays, addition of ATP (and ADP to a less extent) showed an enhanced cytochrome c oxidase activity. Both electron paramagnetic resonance and fluorescence spectra indicate that there is no Significant change in the cytochrome c-cytochrome c oxidase interaction. Instead, reduction levels of the cytochromes at steadystate suggest that the increased activity of nucleotide-bound cytochrome c oxidase is due to faster electron transfer from cytochrome ${\alpha}$ to cytochrome ${\alpha}_3$, which is known to be the fate limiting step in the oxygen reduction by cytochrome c oxidase.