• Proceedings of the Korean Society of Plant Pathology Conference
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• 1998.06a
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• pp.164-165
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• 1998

• Journal of Life Science
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• v.8 no.2
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• pp.119-125
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• 1998

Column-purified double-stranded RNA binding factor (RBF) protein was tested for its binding affinity for the different forms of nucleic acids structure such as single-stranded(ss) and double-stranded(ds)RNA and ss- and dsDNA. The RBF protein was incubated with each of these nucleic acid structures in separate reactions and its comparative binding affnity was visualized by SDS-polyacrylamide gel electrophoresis. The RBF protein bound to the dsRNA molecule to form a tight RNA:protein complex in agreement with previous studies, but not to the other nucleic acid molecules confirming its distinctive affinity for the dsRNA structure. In phosphorylation assay in vito, the purified RBF protein significantly inhibited the autophosphorylation of the PKR derived from not only human but mouse source in the presence of poly(I):poly(C). It is suggesting that PKR vs. RBF is similarly under a competitive interaction among different eukaryotic organisms during protein synthesis.

• Applied Biological Chemistry
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• v.39 no.5
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• pp.379-383
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• 1996

The ultrastructure of the compound starch granules and the protein bodies of Odaebyeo rice of early matured variety were examined by light microscope and electron microscope. The endosperm cell appealed rectangular or octangular shape on the cross section. The thickness of cell wall containing of membraneous materials was about $0.5\;{\mu}m$ in diameter. The starch cell was filled compactly with globular or oval shaped compound starch granules with the size of $20{\sim}25\;{\mu}m$ in diameter. The compound starch granules were consisted of central core starch granule and concentrical $2{\sim}3$ layers of starch granules. The average thickness of the starch granules were about $5\;{\mu}m$. Most protein bodies were found in the aleurone layer The globular protin bodies were scattered near the compound starch granules and $2.5{\sim}3\;{\mu}m$ in diameter. The protein bodies composed of central electron dense materials and peripheral electron loose materials in limiting membrane.

• Journal of the Korea Society of Computer and Information
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• v.14 no.1
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• pp.73-80
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• 2009

G protein-coupled receptors(GPCRs) family is a cell membrane protein, and plays an important role in a signaling mechanism which transmits external signals through cell membranes into cells. But, GPCRs each are known to have various complex control mechanisms and very unique signaling mechanisms. Structural features, and family and subfamily of GPCRs are well known by function. and accordingly, the most fundamental work in studies identifying the previous GPCRs is to classify the GPCRs with given protein sequences. Studies for classifying previously identified GPCRs more easily with mathematical models have been mainly going on. In this paper Considering that functions of proteins are determined by their stereoscopic structures, the present paper proposes a method to compare secondary structures of two GPCRs having different amino acid sequences, and then detect an unknown GPCRs assumed to have a same function in databases of previously identified GPCRs.

• Korean journal of food and cookery science
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• v.20 no.4
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• pp.396-402
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• 2004

The aim of this study was to examine the effect of rice protein on the network structure of the Jeung-Pyun. The major component of Jeung-Pyun rice protein was extracted, the change of rice protein during the Jeung-Pyun fermentation was assessed, and the effect on the viscosity and volume of adding protease to Jeung-Pyun was investigated. In addition, the result of adding protein to rice starch on the viscosity and volume of Jeung-Pyun was that the rice protein mediated the volume and expansion ability. The results were as follows. In rice and dough of Jeung-Pyun, the SDS soluble protein content was higher than that of wheat flour and no change was detected in the amount of extracted protein with the fermentation time. However, in the FPLC pattern, low molecular weight peaks were decreased with the fermentation time, which indicates the increase in the ratio of high molecular weight substances. In contrast, the addition of protease substantially decreased, the viscosity and volume of Jeung-Pyun, whereas the viscosity and volume were increased by adding protein to rice starch in order to reconstitute Jeung-Pyun. This suggested that rice protein in Jeung-Pyun had a mediating effect on both the volume and the formation of the texture.

• Journal of the Computational Structural Engineering Institute of Korea
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• v.20 no.3
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• pp.365-370
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• 2007

Many engineering problems often require the large amount of computing resources for iterative simulations of problems treating many parameters and input files. In order to overcome the situation, this paper proposes an e-Science based computational system. The system exploits the Grid computing technology to establish an integrated web service environment which supports distributed high throughput computational simulations and remote executions. The proposed system provides an easy-to-use parametric study service where a computational service includes real time monitoring. To verify usability of the proposed system, two kinds of applications were introduced. The first application is an Aerospace Integrated Research System (e-AIRS). The e-AIRS adapts the proposed computational system to solve CFD problems. The second one is design and optimization of protein 3-dimensional structures in structural biology.

• Journal of fish pathology
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• v.11 no.1
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• pp.43-50
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• 1998

In order to determine whether the tumor-inducing iridoviruses and the mortality-associated iridoviruses from cultured marine fish in Korea belong to same type, we compared the immunological characteristics of these viruses. The electrophoretical pattern of structural proteins of the tumor-inducing was different from that of the mortality-associated iridoviruses. The antigenicity of structural proteins of these viruses were identified by Western blotting using two monoclonal antibodies against tumor-inducing iridovirus. Two monoclonal antibodies recognized a 150 kDa structural protein of tumor-inducing iridoviruses showed. However, the structural proteins of the mortality-associated iridoviruses did not react with these monoclonal antibodies. These results demonstrate that the antigenicity of the structural proteins of tumor-inducing iridovirus is different from that of mortality-associated iridovirus, indicating that these two iridoviruses belong to different types.

• Journal of Life Science
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• v.31 no.2
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• pp.219-222
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• 2021

In this study, we examined low molecular weight peptides using proteomics in order to identify their original proteins, derive their peptides, and determine the functions of the proteins in Tenebrio molitor, the mealworm (larvae, pupae, or adult) from which the peptides were extracted. Fifty-four proteins were finally identified through an analysis of proteome to derive the analyzed peptides. The proteins that induced low molecular weight peptides were identified to be the most abundant in adults only, and the next highest were derived from a group containing both adults and larva. However, other groups, including pupa, were detected to have a lower frequency of peptides. As a result of orthologous classification of the detected proteins, the general function prediction was only investigated at the highest frequency among the examined proteins. Proteins related to chromatin structure and dynamics were detected by their higher frequency among functional classes. The next highest frequency was shown by proteins related to amino acid transport and metabolism and carbohydrate transport and metabolism. Therefore, it is assumed that proteins correlated with chromatin, amino acid, and carbohydrate metabolisms are easily induced into low molecular weight peptides, and that their peptides could play a role as bioactive substances.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.10
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• pp.1668-1675
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• 2004

The effect of pH on surface hydrophobicity, sulfhydryl group, infrared spectrum, SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) pattern and enthalpy was investigated in recovered protein from mackerel and frozen blackspotted croaker by alkaline processing. Hydrophobic residue in myofibrillar protein exposed to the surface of protein, and hydrophobic interaction were the highest around 6$0^{\circ}C$. The surface hydrophobicity was different between myofibrillar protein and myofibrillar protein including sarcoplasmic protein (recovered protein). The peak at 1636 c $m^{-l}$ was increased with pH, and the recovered protein was unfolded in alkali pH. Difference of surface and total sulfhydryl group at pH 7.0 and 10 was comparative high, and decrease of surface sulfhydryl group indicated formation of S-S bonds. Mackerel and frozen blackspotted croaker in alkaline pH showed bands of polymerized myosin heavy chain on SDS-PAGE pattern. The transition temperatures of recovered protein were 33.1, 44.3 and 65.5$^{\circ}C$. Gelation of recovered protein from alkali processing was estimated by increase of $\beta$-sheet structure by pH treatment, S-S bonds by oxidation of surface sulfhydryl group in heating, polymerization of myosin heavy chain in order.r.

• Korean Journal of Food Science and Technology
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• v.16 no.3
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• pp.279-284
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• 1984

Microstructure of milk powder and cheese made from milk powder were observed by electron microscope. Freeze dried milk powder showed apple-like appearance. The cheese made from freeze dried milk powder had relatively flat surface and homogenous deposit in compare with classical processed cheese. Imported milk powder also indicated similar surface as well as freeze dried milk powder, however, the cheese made from imported milk powder had somewhat coarse surface structures with the spaces between casein matrix and deposit. Commericial milk powder showed irregular shape in size and coagulum which were possibly denatured in the course of drying. The cheese made from commercial powder indicted irregular and small deposit and porous structure. The porousity of the cheese seemed to be influenced by the degree of heat treatment. Denatured protein would be less dispersive than native in presence of polyphosphates. Fat globule and protein micelle of cheese made from skim milk powder get very adjacent to each other and showed compactness of micelles. It is thought that melting mechanism of skim milk powder was different from the melting of typical processed cheese.