• The Korean Journal of Ceramics
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• v.7 no.1
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• pp.30-35
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• 2001

The contribution of the non-$180^{\circ}C$ domains to the electric-field-induced strains (EFI-strains) of PZT ceramics was evaluated by an XRD method and by an interferometric method. The XRD intensity ratio of 200 and 002 diffraction peaks of tetragonal PZT was measured under strong electric fields. The amount of the $90^{\circ}$ domain reorientation was evaluated and the strain due to the domain reorientation was calculated. It was confirmed that the EFI-strain of PZT ceramics was equal to the sum of the strain calculated from the d$_33$ constant determined by the resonance-antiresonance method and the strain due to the $90^{\circ}$ domain reorientation. The amount of the $90^{\circ}$domain reorientation has a linear relation with the c/a ratio in the "soft" PZT ceramics. A Mech-Zehnder interferometer was constructed to measure the EFI-strains vs. electric-field curves of PZT ceramics as a function of frequency. The EFI-strain vs. electric-field curve showed a hysteresis due to the effect of the non-$180^{\circ}$ domain reorientation when the applied voltage was high and its frequency was low. The apparent piezoelectric constant increased from the d$_33$ value determined by the resonance-antiresonance method with decreasing frequency. This deviation was attributed to the non-$180^{\circ}$ domain contribution.tribution.

• The Journal of Korean Institute of Communications and Information Sciences
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• v.28 no.5C
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• pp.461-467
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• 2003

We propose an efficient method for separable symmetric linear filtering in the DCT domain. First, separable 2-D linear filtering is decomposed into the cascade of 1-D filtering in the DCT domain. We investigate special characteristics of DCT domain filtering matrices when the filter coefficients are symmetric. Then we present the DCT domain 2-D filtering method using these characteristics. The proposed method requires smaller number of multiplications including typical sparseness of DCT coefficients compared to previous DCT domain linear filtering methods. Also, the proposed method is composed of simple and regular operations, which would be appropriate for efficient VLSI implementation.

• Communications of the Korean Mathematical Society
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• v.10 no.1
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• pp.145-153
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• 1995

A Jordan domain D in C is said to be a c-quasidisk if there exists a constant $c \geq 1$ such that each two points $z_1$ and $z_2$ in D can be joined by an arc $\tau$ in D such that $$ \ell(\tau) \leq c$\mid$z_1 - z_2$\mid$ $$ and $$ (1.1) min(\ell(\tau_1),\ell(\tau_2)) \leq c d(z, \partial D) $$ for all $z \in \tau$, where $\tau_1$ and $\tau_2$ are the components of $\tau\{z}$. Quasidisks have been extensively studied and can be characterized in many different ways [1],[2],[3].

• The Transactions of the Korean Institute of Electrical Engineers C
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• v.52 no.9
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• pp.412-417
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• 2003

In this Paper, we propose a time-domain magnetic field integral equation (TD-MFIE) formulation for analyzing the transient electromagnetic response from three-dimensional (3-D) dielectric bodies. The solution method in this paper is based on the Galerkin's method that involves separate spatial and temporal testing procedures. Triangular patch basis functions are used for spatial expansion and testing functions for arbitrarily shaped 3-D dielectric structures. The time-domain unknown coefficients of the equivalent electric and magnetic currents are approximated tv a set of orthonormal basis function that is derived from the Laguerre polynomials. These basis functions are also used for the temporal testing. Numerical results computed by the proposed method are presented and compared.

• Proceedings of the Korean Society of Applied Pharmacology
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• 2002.07a
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• pp.236-236
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• 2002

Pyruvate dehydrogenase phosphatase (PDP) is a mitochondrial protein serine/threonine phosphatase that catalyzes the dephosphorylation and concomitant reactivation of the pyruvate dehydrogenase componant of the pyruvate dehydrogenase complex (PDC). PDP consists of a Mg$\^$+2/ -dependent and Ca$\^$+2)-stimulated catalytic subunit (PDPc) of Mr 52,600 and a FAD-containing regulatory subunit (PDPr) of Mr 95.600. Catalytic subunit of pyruvate dehydrogenase phosphatase (PDPc) has been suggested to have three major functional domains such as dihydrolipoamide acetyltransferase(E$_2$)-binding domain, regulatory subunit of PDP(PDPr)-binding domain, and calcium-binding domain. In order to identify functional domains, recombinant catalytic subunit of pyruvate dehydrogenase phosphatase (rPDPc) was expressed in E. coli JM101 and purified to near homogeneity using the unique property of PDPc: PDPm binds to the inner lipoyl domain (L$_2$) of E$_2$ of pyruvate dehydrogenase complex (PDC) in the presence of Ca$\^$+2/, not under EGTA. PDPc was limited-proteolysed by trypsin, chymotrypsin, Arg-C, and elastase at pH7.0 and 30$^{\circ}C$ and N-terminal analysis of the fragment was done. Chymotrypsin, trypsin, and elastase made two major framents: N-terminal large fragment, approx. 50kD and C-terminal small fragment, approx. 0 kDa. Arg-C made three major fragments: N-terminal fragment, approx. 35 kD, and central fragment, approx. 15 kD, and C-terminal fragment, approx. 10 kD. This study strongly suggest that PDPc consists of three major functional domains. However, further study should be necessary to identify the functional role.

• Proceedings of the Korean Magnestics Society Conference
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• 2001.04a
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• pp.104-105
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• 2001

• BMB Reports
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• v.40 no.1
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• pp.22-28
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• 2007

MyoD, expressed in skeletal muscle lineages of vertebrate embryo, is one of muscle-specific basic helix-loop-helix (bHLH) transcription factors, which plays a key role in the determination and differentiation of all skeletal muscle lineages. In this study, a cDNA of grass carp MyoD was cloned and characterized from total RNA of grass carp embryos by RT-PCR. The full-length cDNA of grass carp MyoD is 1597 bp. The cDNA sequence analysis reveals an open reading frame of 825 bp coding for a protein of 275 amino acids, which includes a bHLH domain composed of basic domain (1-84th amino acids) and HLH domain (98-142th amino acids), without signal peptide. Then the MyoD cDNA of grass carp was cloned to yeast expression vector pPICZ$\alpha$A and transformed into P. pastoris GS115 strain, the recombinant MyoD protein with a molecular weight of about 31KD was obtained after inducing for 2d with 0.5% methanol in pH 8.0 BMGY medium, and the maximum yield was about 250 mg/L in shaking-flask fermentation. The results were expected to benefit for further studies on the crystal structure and physiological function of fish MyoD.

• Environmental Analysis Health and Toxicology
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• v.17 no.1
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• pp.73-80
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• 2002

Pyruvate dehydrogenase phosphatase (PDP)와 kinase는 당대사시 해당과정에서의 대사 산물인 pyruvate를 acetyl CoA로 만들어 구연산 회로로 진입시켜 주는 효소인 pyruvate dehydrogenase complex (PDC)의 활성을 조절하는 중요한 효소이다. PDP의 catalytic subunit는 PDC의 dihydrolipoamide acetyltransferase (E2), PDP regulatory subunit (PDPr), 그리고 칼슘 결합 도메인 등으로 구성되어 있는 것으로 추측되어지고 있다. 본 연구에서는 그 구조와 기능과의 상관관계를 알아보기 위해 PDPc를 E. coli JM101에서 발현시켜 순수 정제 후 단백분해 효소를 이용한 제한적 가수분해 방법을 이용해 그 구조와 기능과의 상관관계에 대해 연구하고자 하였다 정제된 PDPc는 trypsin, chymotrypsin, Arg-C 그리고 elastase를 이용하여 3$0^{\circ}C$ 그리고 pH 7.0에서 제한적으로 분해시켰으며 각 분해산물의 아미노 말단의 아미노산 배열을 분석하였다. 그 결과 PDPc는 trypsin, chymotrypsin, elastase에 의해 N-terminal의 50 kD과 C-terminal의 10 kD의 두개의 분해산물을 만들었으며, Arg-C에 의해 50kD의 분해산물은 약 35kD와 15kD으로 더 가수분해가 되었다. 이러한 결과로 볼 때 PDPc는 앞에서 추측한데로 세개의 주요한 기능적 도메인으로 이루어져 있음을 알 수 있었다 또한 C-terminal의 10kD은 PDPc의 활성에는 영향을 주지 않는 것으로 밝혀졌으나 다른 도메인의 기능은 더 연구가 되어져야 할 것으로 생각된다.

• Bulletin of the Korean Chemical Society
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• v.30 no.5
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• pp.1039-1042
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• 2009

RNA polymerase II C-terminal domain phosphatase 1 containing ubiquitin like domain (UBLCP1) has been identified as a regulatory molecule of RNA polymerase II. UBLCP1 consists of ubiquitin like domain (UBL) and phosphatase domain homologous with UDP and CTD phosphatase. UBLCP1 was cloned into the E.coli expression vectors, pET32a and pGEX 4T-1 with TEV protease cleavage site and purified using both affinity and gel-filtration chromatography. Domains of UBLCP1 protein were successfully purified as 7 mg/500 mL (UBLCP1, 36.78 KDa), 32 mg/500 mL (UBL, 9 KDa) and 8 mg/500 mL (phosphatase domain, 25 KDa) yielded in LB medium, respectively. Isotope-labeled samples including triple-labeled ($^2H/^{15}N/^{13}C$) UBLCP1 were also prepared for hetero-nuclear NMR experiments. $^{15}N-^{1}H$ 2D-HSQC spectra of UBLCP1 suggest that both UBL and phosphatase domain are properly folded and structurally independent each other. These data will promise us further structural investigation of UBLCP1 by NMR spectroscopy and/or X-ray crystallography.

• Journal of Microbiology and Biotechnology
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• v.9 no.5
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• pp.619-623
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• 1999

The C-terminal starch-binding domain of Bacillus cereus $\beta$-amylase expressed in Escherichia coli was purified and crystallized using the vapor diffusion method. The crystals obtained belong to a space group of $P3_2$ 21 with cell dimensions, a=b=60.20${\AA},\; c=64.92{\AA},\; and \; \gamma = 120^{\circ}$ The structure was determined by the molecular replacement method and refined at 1.95 ${\AA}$, with R-factors of 0.181. The final model of the starch-binding domain comprised 99 amino acid residues and 108 water molecules. The starch-binding domain had a secondary structure of two 4-stranded antiparallel p-sheets similar to domain E of cyclodextrin glucanotransferase and the C-terminal starch-binding domain of glucoamylase. A comparison of the structures of these starch-binding domains revealed that the separated starch-binding domain of Bacillus cereus $\beta-Amylase$had only one starch-binding site (site 1) in contrast to two sites (site 1 and site 2) reported in the domains of cyclodextrin glucanotransferase and glucoamylase.