• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2001.05c
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• pp.143-147
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• 2001

Ferromagnetism in manganese compound semiconductors open prospects for tailoring magnetic and spin-related phenomena in semiconductors with a precision specific to III-V compounds. Also it addresses a question about the origin of the magnetic interactions that lead to a Curie temperature(Tc) as high as 110 K for a manganese concentration of just 5%. Zener's model of ferromagnetism, originally suggested for transition metals in 1950, can explain Tc of $Ga_{1-x}Mn_x$ As and that of its IT-VI counterpart $Zn_{1-x}Mn_x$ Te and is used to predict materials with Tc exceeding room temperature, an important step toward semiconductor electronics that use both charge and spin. In this article, we present not only the experimental result but calculated Curie temperature by RKKY interaction. The problem in making III-V semiconductor has been the low solubility of magnetic elements, such as manganese, in the compound, since the magnetic effects are roughly proportional to the concentration of the magnetic ions. Low solubility of magnetic elements was overcome by low-temperature nonequilibrium MBE{molecular beam epitaxy) growth, and ferromagnetic (Ga,Mn)As was realized. Magnetotransport measurements revealed that the magnetic transition temperature can be as high as 110 K for a small manganese concentration.

• Journal of the Korean Magnetics Society
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• v.27 no.4
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• pp.140-144
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• 2017

We have studied electronic and magnetic structure of cubane-type Co magnetic molecule using density functional method. The calculated density of states show $Co^{+2}$ ionic state and high-spin state because of large exchange interaction between inside Co 3d electrons. The exchange interaction J between Co atoms depends Co-O-Co angle. The calculated J is ferromagnetic with right angles. On the other hand J is antiferromagnetic with large angles since super-exchange interactions between $Co^{+2}$ atoms. It induces that Co cubane has a antiferromagnetic spin structure of AFM1 = [${\uparrow}{\uparrow}{\downarrow}{\downarrow}$]

• Macromolecular Research
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• v.15 no.7
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• pp.646-655
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• 2007

To achieve targeted drug delivery for chemotherapy, a ligand-mediated nanoparticulate drug carrier was designed, which could identity a specific receptor on the surfaces of tumor cells. Biodegradable poly(ethylene oxide)/poly$({\varepsilon}-caprolactone)$ (PEG/PCL) amphiphilic block copolymers coupled to biotin ligands were synthesized with a variety of PEG/PCL compositions. Block copolymeric nanoparticles harboring the anticancer drug paclitaxel were prepared via micelle formation in aqueous solution. The size of the biotin-conjugated PEG/PCL nanoparticles was determined by light scattering measurements to be 88-118 nm, depending on the molecular weight of the block copolymer, and remained less than 120 nm even after paclitaxel loading. From an in vitro release study, biotin-conjugated PEG/PCL nanoparticles containing paclitaxel evidenced sustained release profiles of the drug with no initial burst effect. The biotin-conjugated PEG/PCL block copolymer itself evidenced no significant adverse effects on cell viability at $0.005-1.0{\mu}g/mL$ of nanoparticle suspension regardless of cell type (normal human fibroblasts and HeLa cells). However, biotin-conjugated PEG/PCL harboring paclitaxel evidenced a much higher cytotoxicity for cancer cells than was observed in the PEG/PCL nanoparticles without the biotin group. These results showed that the biotin-conjugated nanoparticles could improve the selective delivery of paclitaxel into cancer cells via interactions with over-expressed biotin receptors on the surfaces of cancer cells.

• Proceedings of the Botanical Society of Korea Conference
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• 1999.07a
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• pp.41-44
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• 1999

Magnaporthe grisea (Hebert) Barr (anamorph: Pyricularia grisea) is a typical heterothallic Ascomycete and the causal agent of rice blast, one of the most destructive diseases on rice (Oryza sativa L.) worldwide. The interactions between cells of the pathogen and those of the host involve a complex of biological influences which can lead to blast disease. The early stages of infection process in particular may be viewed as a sequence of discrete and critical events. These include conidial attachment, gemination, and the formation of an appressorium, a dome-shaped and melanized infection structure. Disruption of this process at any point will result in failure of the pathogen to colonize host tissues. This may offer a new avenue for developing innovative crop protection strategies. To recognize and capture such opportunities, understanding the very bases of the pathogenesis at the cellular and molecular level is prerequisite. Much has been learned about environmental cues and endogenous signaling systems for the early infection-related morphogenesis in M. grisea during last several years. The study of signal transduction system in phytopathogenic filamentous fungi offers distinct advantages over traditional mammalian systems. Mammalian systems often contain multiple copies of important genes active in the same tissue under the same physiological processes. Functional redundancy, alternate gene splicing, and specilized isoforms make defining the role of any single gene difficult. Fungi and animals are closely related kingdoms [3], so inferences between these organisms are often justified. For many genes, fungi frequently possess only a single copy, thus phenotype can be attributed directly to the mutation or deletion of any particular gene of interest.

• Proceedings of the Botanical Society of Korea Conference
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• 1985.08b
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• pp.19-22
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• 1985

Magnaporthe grisea (Hebert) Barr (anamorph: Pyricularia grisea) is a typical heterothallic Ascomycete and the causal agent of rice blast, one of the most destructive diseases on rice (Oryza sativa L.) worldwide. The interactions between cells of the pathogen and those of the host involve a complex of biological influences which can lead to blast disease. The early stages of infection process in particular may be viewed as a sequence of discrete and critical events. These include conidial attachment, gemination, and the formation of an appressorium, a dome-shaped and melanized infection structure. Disruption of this process at any point will result in failure of the pathogen to colonize host tissues. This may offer a new avenue for developing innovative crop protection strategies. To recognize and capture such opportunities, understanding the very bases of the pathogenesis at the cellular and molecular level is prerequisite. Much has been learned about environmental cues and endogenous signaling systems for the early infection-related morphogenesis in M. grisea during last several years. The study of signal transduction system in phytopathogenic filamentous fungi offers distinct advantages over traditional mammalian systems. Mammalian systems often contain multiple copies of important genes active in the same tissue under the same physiological processes. Functional redundancy, alternate gene splicing, and specilized isoforms make defining the role of any single gene difficult. Fungi and animals are closely related kingdoms [3], so inferences between these organisms are often justified. For many genes, fungi frequently possess only a single copy, thus phenotype can be attributed directly to the mutation or deletion of any particular gene of interest.

• Molecules and Cells
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• v.25 no.3
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• pp.352-357
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• 2008

Osteoprotegerin (OPG) is a soluble decoy receptor that inhibits osteoclastogenesis and is closely associated with bone resorption processes. We have designed and determined the solution structures of potent OPG analogue peptides, derived from sequences of the cysteine-rich domain of OPG. The inhibitory effects of the peptides on osteoclastogenesis are dose-dependent ($10^{-6}M-10^{-4}M$), and the activity of the linear peptide at $10^{-4}M$ is ten-fold higher than that of the cyclic OPG peptide. Both linear and cyclic peptides have a ${\beta}$-turn-like conformation and the cyclic peptide has a rigid conformation, suggesting that structural flexibility is an important factor for receptor binding. Based on structural and biochemical information about RANKL and the OPG peptides, we suggest that complex formation between the peptide and RANKL is mediated by both hydrophobic and hydrogen bonding interactions. These results provide structural insights that should aid in the design of peptidyl-mimetic inhibitors for treating metabolic bone diseases caused by abnormal osteoclast recruitment.

• Proceedings of the Korean Biophysical Society Conference
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• 2003.06a
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• pp.66-66
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• 2003

In skeletal muscle cells, depolarization of the transverse tubules (T-tubules) results in Ca$\^$2+/ release from the sarcoplasmic reticulum (SR), leading to elevated cytoplasmic Ca$\^$2+/ and muscle contraction. This process has been known as excitation-contraction coupling (E-C coupling). Several proteins, such as the ryanodine receptor (RyR), triadin, junctin, and calsequestrin (CSQ), have been identified to be involved in the Ca$\^$2＋/ release process. However, the molecular interactions between the SR proteins have not been resolved. In the present study, the mechanisms of interaction between RyRl and triadin have been studied by in vitro protein binding and $\^$45/Ca$\^$2+/ overlay assays. Our data demonstrate that the intraluminal loop II of RyR1 binds to triadin in Ca$\^$2+/-independent manner. Moreover, we could not find any Ca$\^$2+/ binding sites in the loop II region. GST-pull down assay revealed that a KEKE motif of triadin, which was previously identified as a CSQ binding site (Kobayasi et al.,2000 JBC) was also a binding site for RyR1. Our results suggest that the intraluminal loop II of RyR could participate in the RyR-mediated Ca$\^$2+/ release process by offering a direct binding site to luminal triadin.

• Proceedings of the Korean Biophysical Society Conference
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• 2003.06a
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• pp.53-53
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• 2003

Calumenin was previously identified as a high affinity Ca$\^$2+/ binding protein in mouse cardiac sarcoplasmic reticulum (SR). For the present study, a 48 kDa skeletal homologue of calumenin was identified by sucrose-density gradient of rabbit skeletal SR membranes, concanavalin A treatment, 2D-gel electrophoresis, $\^$45/Ca$\^$2+/ overlay, Stains-all staining, and MALDI-TOF analysis. We attempted to clone the skeletal calumenin by RT-PCR based on mouse cardiac and human calumenin sequences. The deduced amino acid sequence (315 residues) of the skeletal calumenin showed high identity to mouse cardiac calumenin (90％). As seen in the cardiac calumenin, the deduced sequence contains a 19 amino acid N-terminal signal sequence and a HDEF C-terminal sequence, a putative retrieval signal to ER. Also, the skeletal calumenin contains one N-glycosylation site, three PKC phosphorylation sites, eight casein kinase 2 phosphorylation sites, and 6 EF-hand domains. GST-calumenin showed a conformational change and increased mobility in the presence of Ca$\^$2+/ in SDS-PAGE. Three calumenin interacting proteins (ryanodine receptor 1, glycogen phosphorylase, and phosphofructo kinase) were identified by pull-down assay with GST-calumenin and solubilized SR. All the interactions were Ca$\^$2+/dependent. The present results suggest that calumenin plays an important role in Ca$\^$2+/ homeostasis of muscle cells.

• Bulletin of the Korean Chemical Society
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• v.33 no.11
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• pp.3719-3726
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• 2012

Formation of Z-DNA, a left-handed double helix, from B-DNA, the canonical right-handed double helix, occurs during important biological processes such as gene expression and DNA transcription. Such B-Z transitions can also be induced by high salt concentration in vitro, but the changes in the relative stability of B-DNA and Z-DNA with salt concentration have not been fully explained despite numerous attempts. For example, electrostatic effects alone could not account for salt-induced B-Z transitions in previous studies. In this paper, we propose that the B-Z transition can be explained if counterion entropy is considered along with the electrostatic interactions. This can be achieved by conducting all-atom, explicit-solvent MD simulations followed by MM-PBSA and molecular DFT calculations. Our MD simulations show that counterions tend to bind at specific sites in B-DNA and Z-DNA, and that more ions cluster near Z-DNA than near B-DNA. Moreover, the difference in counterion ordering near B-DNA and Z-DNA is larger at a low salt concentration than at a high concentration. The results imply that the exclusion of counterions by Z-DNA-binding proteins may facilitate Z-DNA formation under physiological conditions.

• Bulletin of the Korean Chemical Society
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• v.31 no.10
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• pp.2877-2883
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• 2010

The folding kinetics of $WT^*$ ubiquitin variant with valine to alanine mutation at sequence position 26 (HubWA) was studied by stopped-flow fluorescence spectroscopy. While unfolding kinetics showed a single exponential phase, refolding reaction showed three exponential phases. The semi-logarithmic plot of urea concentration vs. rate constant for the first phase showed v-shape pattern while the second phase showed v-shape with roll-over effect at low urea concentration. The rate constant and the amplitude of the third phase were constant throughout the urea concentrations, suggesting that this phase represents parallel process due to the configurational isomerization. Interestingly, the first and second phases appeared to be coupled since the amplitude of the second phase increased at the expense of the amplitude of the first phase in increasing urea concentrations. This observation together with the roll-over effect in the second folding phase indicates the presence of intermediate state during the folding reaction of HubWA. Quantitative analysis of Hub-WA folding kinetics indicated that this intermediate state is on the folding pathway. Folding kinetics measurement of a mutant HubWA with hydrophobic core residue mutation, Val to Ala at residue position 17, suggested that the intermediate state has significant amount of native interactions, supporting the interpretation that the intermediate is on the folding pathway. It is considered that HubWA is a useful model protein to study the contribution of residues to protein folding process using folding kinetics measurements in conjunction with protein engineering.