• Journal of the Korea Institute of Information Security & Cryptology
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• v.28 no.5
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• pp.1141-1151
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• 2018

In an APT attack, the communication stage between infected hosts and C&C(Command and Control) server is the key stage for intrusion into the attack target. Attackers can control multiple infected hosts by the C&C Server and direct intrusion and exploitation. If the C&C Server is exposed at this stage, the attack will fail. Therefore, in recent years, the Domain Generation Algorithm (DGA) has replaced DNS in C&C Server with a short time interval for making detection difficult. In particular, it is very difficult to verify and detect all the newly registered DNS more than 5 million times a day. To solve these problems, this paper proposes a model to judge DGA-DNS detection by the morphological similarity analysis of normal DNS and DGA-DNS, and to determine the sign of APT attack through it, then we verify its validity.

• Korea-Australia Rheology Journal
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• v.12 no.3_4
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• pp.175-179
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• 2000

Rheological properties of chitosan solutions were investigated as a function of polymer concentration. The viscosity curves for chitosan solutions consisted of two distinct viscosity regions, the Newtonian zero-shear viscosity (η$_{0}$) region and the shear rate dependent apparent viscosity (η$_{app}$) region. The shear rate dependence of viscosity was more clearly observed at higher chitosan concentrations. The critical coil overlap parameter (C＊〔η〕) was determined to be approximately 3.2 from a plot of zero-shear specific viscosity η$_{sp,0}$ vs coil overlap parameter (C〔η〕), which was lower than C〔η〕4.0 reported for other random coil polysaccharides. It was also found that the slope of η$_{sp,0}$ vs C〔η〕 was 3.9 at concentrated C〔η〕>C＊〔η〕domain, while 1.2 at dilute C〔η〕$_{0}$ ${\gamma}$/${\gamma}$$_{0.8}$ relation.ion.n.n.

• The Transactions of the Korean Institute of Electrical Engineers C
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• v.51 no.11
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• pp.551-558
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• 2002

A time-domain combined field integral equation (CFIE) is presented to obtain the transient scattering response from arbitrarily shaped three-dimensional conducting bodies. This formulation is based on a linear combination of the time-domain electric field integral equation (EFIE) with the magnetic field integral equation (MFIE). The time derivative of the magnetic vector potential in EFIE is approximated using a central finite difference approximation and the scalar potential is averaged over time. The time-domain CFIE approach produces results that are accurate and stable when solving for transient scattering responses from conducting objects. The incident spectrum of the field may contain frequency components, which correspond to the internal resonance of the structure. For the numerical solution, we consider both the explicit and implicit scheme and use two different kinds of Gaussian pulses, which may contain frequencies corresponding to the internal resonance. Numerical results for the EFIE, MFIE, and CFIE are presented and compared with those obtained from the inverse discrete Fourier transform (IDFT) of the frequency-domain CFIE solution.

• BMB Reports
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• v.46 no.1
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• pp.37-40
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• 2013

CY-007 and CY-049 pteridine glycosyltransferases (PGTs) that differ in sugar donor specificity to catalyze either glucose or xylose transfer to tetrahydrobiopterin were studied here to uncover the structural determinants necessary for the specificity. The importance of the C-terminal domain and its residues 218 and 258 that are different between the two PGTs was assessed via structure-guided domain swapping or single and dual amino acid substitutions. Catalytic activity and selectivity were altered in all the mutants (2 chimeric and 6 substitution) to accept both UDP-glucose and UDP-xylose. In addition, the wild type activities were improved 1.6-4.2 fold in 4 substitution mutants and activity was observed towards another substrate UDP-N-acetylglucosamine in all the substitution mutants from CY-007 PGT. The results strongly support essential role of the C-terminal domain and the two residues for catalysis as well as sugar donor specificity, bringing insight into the structural features of the PGTs.

• Bulletin of the Korean Chemical Society
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• v.29 no.5
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• pp.1013-1017
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• 2008

Syndecan-3 is a cell-surface heparan sulfate proteoglycan, which performs a variety of functions during cell adhension process. It is also a coreceptor for growth factor, mediating cell-cell and cell-matrix interaction. Syndecan-3 contains a cytoplasmic domain potentially associated with the cytoskeleton. Syndecan-3 is specifically expressed in neuron cell and has related to neuron cell differentiation and development of actin filament in cell migration. Syndecans each have a unique, central, and variable (V) region in their cytoplasmic domains. And that region of syndecan-3 may modulate the interactions of the conserved C1 regions of the cytoplasmic domains by tyrosine phosphorylation. Cytoplasmic domain of syndecan-3 has been synthesized for NMR structural studies. The solution structure of syndecan-3 cytoplasmic domain has been determined by two-dimensional NMR spectroscopy and simulated-annealing calculation. The cytoplasmic domain of the syndecan proteins has a tendency to form a dimmer conformation with a central cavity, however, that of syndecan-3 demonstrated a monomer conformation with a flexible region near C-terminus. The structural information might add knowledge about the structure-function relationships among syndecan proteins.

• Journal of Microbiology and Biotechnology
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• v.26 no.2
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• pp.226-232
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• 2016

Dihydrodipicolinate reductase is an enzyme that converts dihydrodipicolinate to tetrahydrodipicolinate using an NAD(P)H cofactor in L-lysine biosynthesis. To increase the understanding of the molecular mechanisms of lysine biosynthesis, we determined the crystal structure of dihydrodipicolinate reductase from Corynebacterium glutamicum (CgDapB). CgDapB functions as a tetramer, and each protomer is composed of two domains, an Nterminal domain and a C-terminal domain. The N-terminal domain mainly contributes to nucleotide binding, whereas the C-terminal domain is involved in substrate binding. We elucidated the mode of cofactor binding to CgDapB by determining the crystal structure of the enzyme in complex with NADP⁺ and found that CgDapB utilizes both NADH and NADPH as cofactors. Moreover, we determined the substrate binding mode of the enzyme based on the coordination mode of two sulfate ions in our structure. Compared with Mycobacterium tuberculosis DapB in complex with its cofactor and inhibitor, we propose that the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme.

• Biodesign
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• v.5 no.4
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• pp.136-140
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• 2017

Lam6 is a member of sterol-specific ${\underline{l}ipid$ transfer proteins ${\underline{a}}nchored$ at ${\underline{m}ebrane$ contact sites (LAMs). Lam6 localizes to the ER-mitochondria contact sites by its PH-like domain and the C-terminal transmembrane helix. Here, we purified and crystallized the Lam6 PH-like domain from Saccharomyces cerevisiae. To aid crystallization of the Lam6 PH-like domain, T4 lysozyme was fused to the N-terminus of the Lam6 PH-like domain with a short dipeptide linker, GlySer. The fusion protein was crystallized under the condition of 0.1 M HEPES-HCl pH 7.0, 10% (w/v) PEG 8000, and 0.1 M $Na_3$ Citrate at 293K. X-ray diffraction data of the crystals were collected to $2.4{\AA}$ resolution using synchrotron radiation. The crystals belong to the orthorhombic space group $P2_12_12_1$ with unit cell parameters $a=59.5{\AA}$, $b=60.1{\AA}$, and $c=105.6{\AA}$. The asymmetric unit contains one T4L-Lam6 molecule with a solvent content of 58.7%. The initial attempt to solve the structure by molecular replacement using the T4 lysozyme structure was successful.

• Transactions of the Korean Society of Mechanical Engineers A
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• v.24 no.1 s.173
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• pp.240-249
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• 2000

An improved global optimization algorithm is developed by extending the domain elimination method. The concept of triangular patch consists of two or more trajectories of local minimizations is introduced to widen the attraction region of the domain elimination method. Using the an-]c between each of three vertices of the patch and a design point, we measure the proximity, between the design point and the patch. With the Gram-Schimidt orthonormalization, this method can be extended to general n-dimensional problems. We code the original domain elimination algorithm and a patch-based algorithm. Then we compare the performance of two algorithms. Through the well-known example problems. the algorithm using patch is shown to be superior to the original domain elimination algorithm in view of computational efficiency.

• Journal of Magnetics
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• v.15 no.4
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• pp.169-172
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• 2010

The coercivity mechanism in permanent magnets was analyzed according to the effects of domain nucleation and domain wall pinning. The coercivity mechanism of a TbCo thin film with high perpendicular magnetic anisotropy was considered in terms of the local inhomogeneity in the thin film. The initial magnetization curves of the TbCo thin films demonstrated domain wall pinning to be the main contributor to the coercivity mechanism than domain nucleation. Based on the coercivity model proposed by Kronmuller et al., the inhomogeneity size acting as a domain wall pinning site was determined. Using the measured values of perpendicular anisotropy constant ($K_u$), saturation magnetization ($M_s$), and coercivity ($H_c$), the inhomogeneity size estimated in a TbCo thin film with high coercivity was approximately 9 nm.

• BMB Reports
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• v.35 no.3
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• pp.343-347
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• 2002

The human protein tyrosine kinase-6 (PTK6) polypeptide that is deduced from the cDNA sequence contains a Src homology (SH) 3 domain, SH2 domain, and catalytic domain of tyrosine kinase. We initiated biochemical and NMR characterization of PTK6 SH3 domain in order to correlate the structural role of the PTK6 using circular dichroism and heteronuclear NMR techniques. The circular dichroism data suggested that the secondary structural elements of the SH3 domain are mainly composed of $\beta$-sheet conformations. It is most stable when the pH is neutral based on the pH titration data. In addition, a number of cross peaks at the low-field area of the proton chemical shift of the NMR spectra indicated that the PTK6 SH3 domain retains a unique and folded conformation at the neutral pH condition. For other pH conditions, the SH3 domain became unstable and aggregated during NMR measurements, indicating that the structural stability is very sensitive to pH environments. Both the NMR and circular dichroism data indicate that the PTK6 SH3 domain experiences a conformational instability, even in an aqueous solution.