• Bulletin of the Korean Chemical Society
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• v.32 no.8
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• pp.2607-2610
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• 2011

Monodispersed Ag/$TiO_2$ core/shell nanoparticles were synthesized in solution via colloid-seeded deposition process using Ag nanoparticles as colloid seeds and $Ti(SO_4)_2$ as Ti-source respectively. Silver nitrate was reduced to Ag nanoparticles with $N_2H_4{\cdot}H_2O$ in the presence of CTAB as stabilizing agent. The titania sols hydrolyzed by the $Ti(SO_4)_2$ solution deposited on the surface of Ag nanoparticles to form the Ag/$TiO_2$ core/shell nanoparticles. Inductively coupled plasma atomic emission spectrometry (ICP-AES) showed low amount of Ag ion leaching from the Ag/$TiO_2$ core/shell nanoparticles. The Ag/$TiO_2$ core/shell nanoparticles indicated excellent antibacterial effects against Escherichia coli and maintained long-term antibacterial property.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2001.11b
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• pp.3-6
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• 2001

In common globular proteins, the native form is in its most stable state. However, the native form of inhibitory serpins (serine protease inhibitors) and some viral membrane fusion proteins is in a metastable state. Metastability in these proteins is critical to their biological functions. Our previous studies revealed that unusual interactions, such as side-chain overpacking, buried polar groups, surface hydrophobic pockets, and internal cavities are the structural basis of the native metastability. To understand the mechanism by which these structural defects regulate protein functions, cavity-filling mutations of a 1-antitrypsin, a prototype serpin, were characterized. Increasing conformational stability is correlated with decreasing inhibitory activity. Moreover, the activity loss appears to correlate with the decrease in the rate of the conformational switch during complex formation with a target protease. We also increased the stability of a 1-antitrypsin greatly via combining various stabilizing single amino acid substitutions that were distributed throughout the molecule. The results showed that a substantial increase of stability, over 13 kcal/mol, affected the inhibitory activity with a correlation of 11% activity loss per kcal/mol. The results strongly suggest that the native metastability of proteins is indeed a structural design that regulates protein functions and that the native strain of a 1-antitrypsin distributed throughout the molecule regulates the inhibitory function in a concerted manner.

• Journal of the Korean Society for Precision Engineering
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• v.27 no.2
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• pp.34-39
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• 2010

In order to achieve and maintain dimensional accuracy in laser micro-machining, dominant parameters such as laser power and laser focus position need to be monitored and controlled real time. Also, in order to selectively machine multi-layered materials, the material being presently machined need to be recognized. This paper presents an auto-focusing (AF) module to keep laser focus on a large-area surface; a real-time laser power stabilizing module based on optical attenuation; and a laser-induced breakdown spectroscopy (LIBS) module. With these monitoring modules, position error in laser focus on a 4" silicon wafer was kept below $4{\mu}m$, initially $51{\mu}m$, and laser power stability of a UV laser source was improved from 1.6% to 0.3%. Also, the material transition from polyimide to copper in machining of FCCL (flexible copper clad laminate) was successfully observed.

• Electrical & Electronic Materials
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• v.14 no.12
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• pp.3-6
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• 2001

In common globular proteins, the native form is n its most stable state. However, the native form of inhibitory serpins (serine protease inhibitors) and some viral membrane fusion proteins is in a metastable state. Metastability in these proteins is critical to their biological functions. Our previous studies revealed that unusual interactions, such as side-chain overpacking, buried polar groups, surface hydrophobic pockets, ad internal cavities are the structural basis of the native metastability. To understand the mechanism by which these structural defects regulate protein functions, cavity-filling mutations of $\alpha$1-antitrypsin, a prototype serpin, were characterized. Increasing conformational stability is correlated with decreasing inhibitory activity. Moreover, the activity loss appears to correlate with the decrease in the rate of the conformational switch during complex formation with a target protease. We also increased the stability of $\alpha$1-antitrypsin greatly via combining various stabilizing single amino acid substitutions that were distributed throughout the molecule. The results showed that a substantial increase of stability, over 13 kcal/mol, affected the inhibitory activity with a correlation of 11% activity loss per kcal/mol. The results strongly suggest that the native metastability of proteins is indeed a structural design that regulates protein functions and that the native strain of $\alpha$1-antitrypsin distributed throughout the molecule regulates the inhibitory function in a concerted manner.

• Journal of the Korean Institute of Electrical and Electronic Material Engineers
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• v.16 no.12S
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• pp.1181-1186
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• 2003

Chemical Mechanical Polishing (CMP) is an essential dielectric planarization in multilayer microelectronic device fabrication. In the CMP process, it is necessary to minimize the extent of surface defect formation while maintaining good planarity and optimal material removal rates. The polishing mechanism of W-CMP process has been reported as the repeated process of passive layer formation by oxidizer and abrasion action by slurry abrasives. Thus, it is important to understand the effect of oxidizer on W passivation layer, in order to obtain higher removal rate (RR) and very low non-uniformity (NU %) during W-CMP process. In this paper, we compared the effects of oxidizer or W-CMP process with three different kind of oxidizers with 5 wt% hydrogen peroxide such as Fe(NO$_3$)$_3$, H$_2$O$_2$, and KIO$_3$. The difference in removal rate and roughness of W in stable and unstable slurries are believed to caused by modification in the mechanical behavior of Al$_2$O$_3$ particles in presence of surfactant stabilizing the slurry.

• Journal of the Microelectronics and Packaging Society
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• v.7 no.3
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• pp.27-29
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• 2000

For the DLC-coaled Si-tip FEA, the modified lift off-process, by which DLC coated on both gate electrode surface and gate insulator in the gate aperture could be removed, was proposed. In the process, the Al sacrificial layer was deposited on a tilted and rotated substrate by an e-beam evaporation, and DLC film was coated on the substrate by PA-CVD method. Afterward the DLC was perfectly removed except the DLC films coated on emitter tips by etch-out of Al sacrificial layer. Current-voltage curves and current fluctuation of the DLC-coated Si-tip FEA showed that the proposed lift-off process played an important role in decreasing gate leakage current and stabilizing omission current.

• Bulletin of the Korean Chemical Society
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• v.30 no.8
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• pp.1733-1737
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• 2009

A new cathode material based on Li$Ni_{0.8}Co_{0.15}Al_{0.05}O_2$ (LNCA)/polyaniline (Pani) composite was prepared by in situ self-stabilized dispersion polymerization in the presence of LNCA. The materials were characterized by fourier transform infrared spectroscopy (FT-IR), ultraviolet-visible spectroscopy (UV-Vis), X-ray diffraction (XRD), and scanning electron microscopy (SEM). Electrochemical properties including galvanostatic charge-discharge ability, cyclic voltammetry (CV), capacity, cycling performance, and AC impedance were measured. The synthesized LNCA/Pani had a similar particle size to LNCA and exhibited good electrochemical properties at a high C rate. Pani (the emeraldine salt form) interacts with metal-oxide particles to generate good connectivity. This material shows good reversibility for Li insertion in discharge cycles when used as the electrode of lithium ion batteries. Therefore, the Pani coating is beneficial for stabilizing the structure and reducing the resistance of the LNCA. In particular, the LNCA/Pani material has advantageous electrochemical properties.

• Geomechanics and Engineering
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• v.6 no.3
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• pp.277-292
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• 2014

Soil nailing, as an effective stabilizing method for slopes and excavations, has been widely used worldwide. However, the interaction mechanism of a soil nail and the surrounding soil and its influential factors are not well understood. A pullout model using a hyperbolic shear stress-shear strain relationship is proposed to describe the load-deformation behavior of a cement grouted soil nail. Numerical analysis has been conducted to solve the governing equation and the distribution of tensile force along the nail length is investigated through a parametric study. The simulation results are highly consistent with laboratory soil nail pullout test results in the literature, indicating that the proposed model is efficient and accurate. Furthermore, the effects of key parameters, including normal stress, degree of saturation of soil, and surface roughness of soil nail, on the model parameters are studied in detail.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2001.11a
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• pp.3-6
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• 2001

In common globular proteins, the native form is in its most stable state. However, the native form of inhibitory serpins (serine protease inhibitors) and some viral membrane fusion proteins is in a metastable state. Metastability in these Proteins is critical to their biological functions. Our previous studies revealed that unusual interactions, such as side-chain overpacking, buried polar groups, surface hydrophobic pockets, and internal cavities are the structural basis of the native metastability. To understand the mechanism by which these structural defects regulate protein functions, cavity-filling mutations of ${\alpha}$1-antitrypsin, a prototype serpin, were characterized. Increasing conformational stability is correlated with decreasing inhibitory activity. Moreover, the activity loss appears to correlate with the decrease in the rate of the conformational switch during complex formation with a target protease. We also increased the stability of ${\alpha}$1-antitrypsin greatly via combining various stabilizing single amino acid substitutions that were distributed throughout the molecule. The results showed that a substantial increase of stability, over 13 kcal/mol, affected the inhibitory activity with a correlation of 11% activity loss per kcal/mol. The results strongly suggest that the native metastability of proteins is indeed a structural design that regulates protein functions and that the native strain of e 1-antitrypsin distributed throughout the molecule regulates the inhibitory function in a concerted manner.

• Bulletin of the Korean Chemical Society
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• v.12 no.2
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• pp.143-148
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• 1991

In the unhydrated and hydrated states, conformational free energies of L-ascorbic acid anion (AAA) were computed with an empirical potential function and the hydration shell model (a program CONBIO). The conformational energy was minimized from possible starting conformations expressed with five torsion angles of the molecule. The conformational entropy of each low energy conformation in both states was computed using a harmonic approximation. As found in L-ascorbic acid (AA), intramolecular hydrogen bonds (HBs) are proved to be of significant importance in stabilizing the overall conformations of AAA in both states, and give the folded conformations, which are quite different from those in crystal. There are competitions between HBs and hydration around O3 atom of the lactone ring and hydroxyls of the acyclic side chain. Especially, the whole conformation of AAA is strongly dependent on the water-accessibility of O3 atom. Though there is a significant effect of the hydration on conformational surface, the lowest energy conformation of the unhydrated AAA is conserved. The different patterns of HBs and hydration result in the conformations of AAA in both states being different from those of AA. It can be drawn by several feasible conformations obtained in the hydrated state that there exists an ensemble of several conformations in aqueous solution.