• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.47 no.4
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• pp.38-45
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• 2015

Fold cracking is one of quality troubles of coated papers. In this study, the fold cracking of high grammage ($250g/m^2$) coated paper made with the different pulp composition and layer structure of base paper was investigated. The single layered, high grammage base paper was prepared by mixing of hardwood and softwood bleached kraft pulp fibers with the different ratios. The high grammage coated paper showed the higher fold cracking than low grammage coated paper because of the increase in thickness. The increase in the content of softwood pulp fibers reduced the fold cracking in the case of high grammage coated paper. When the creasing process was conducted before folding process, the fold cracking of coated paper decreased. By manufacturing the base paper with multiply structure, the fold cracking of coated paper could be reduced significantly, especially when the BCTMP and OCC were used as a middle layer and the creasing process was carried out. The delamination of layers in base paper affected the fold cracking positively.

• BMB Reports
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• v.33 no.3
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• pp.195-201
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• 2000

A human gene has been reported that may encode the enzyme acetohydroxyacid synthase. Previously this enzyme was thought to be absent from animals although it is present in plants and many microorganisms. In plants, this enzyme is the target of a number of commercial herbicides and the use of these compounds may need to be reassessed if the human enzyme exists and proves to be susceptible to inhibition. Here we report the construction of several plasmid vectors containing the cDNA sequence for this protein, and their expression in Escherichia coli. High levels of expression were observed, but most of the protein proved to be insoluble. The small amounts of soluble protein contained little or no acetohydroxyacid synthase activity. Attempts to refold the insoluble protein were successful insofar as the protein became soluble. However, the refolded protein did not gain any acetohydroxyacid synthase activity. In vivo complementation tests of an E. coli mutant produced no evidence that the protein is active. Incorrect folding, or the lack of another subunit, may explain the data but we favor the interpretation that this gene does not encode an acetohydroxyacid synthase.

• Journal of architectural history
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• v.28 no.2
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• pp.7-18
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• 2019

The Chosun Dynasty established and implemented measures to prevent Japanese invasion into the southern coast. To this end, the number of naval vessels and the number of ships were increased, and a shipyard(船所) was constructed to protect the safety of the vessels. The shipyard is a port facility where military vessels are anchored and repaired, as well as public facilities that are needed for military training on public and land, as well as facilities for storing supplies and equipment needed for ships on land and defense at the port entrance. Despite being such an important facility for national defense, Shipyard has not been noticed. Studies have shown that the position of shipyard is divided into the riverside type and the riverbank type, which is due to the topographical features of Korea. The repair cycle of naval vessels, the carrying out of Yeonhun(prevent the water from decaying the part of the ship, a raw tree was burned to smoke) and the place of sea training also affected the construction of the Gul River(掘江). The space structure of shipyard is divided into port entry facilities for monitoring and controlling at the entrance to the harbor, border facilities for folding and repairing military vessels, and land facilities for holding land exercises and administrative work of military vessels and military equipment.

• The Korean Journal of Petroleum Geology
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• v.1 no.1 s.1
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• pp.53-62
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• 1993

The geologic structure of the Yongil Bay was studied in detail based on high resolution seismic profiles. The seafloor trends NE to SW with a deeper part off the Kuryong Peninsula. The seafloor is rather smooth due to the Quaternary fluvial deposits in the lower part and muddy sediments in the upper part. The seafloor off Umockri is very irregular due to erosion where Tertiary sedimentary rocks crop out. The underlying basement rocks were strongly deformed with faults and folds. High-angled reverse faults mostly trend N-S and NNW-SSE and are indicative of westward thrusting. Normal faults in NW-SE and WNW-ESE directions occur locally. Large folding structures trend NE-SW nearshore area of Umockri. The geologic structure suggests that the bay was subject to compressional stress regimes trending E-W and/or NW-SE prior to the early Late Miocene.

• Fashion & Textile Research Journal
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• v.24 no.6
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• pp.667-685
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• 2022

This paper aims to investigate 4D printing materials for soft robots. 4D printing is a targeted evolution of the 3D printed structure in shape, property, and functionality. It is capable of self-assembly, multi-functionality, and self-repair. In addition, it is time-dependent, printer-independent, and predictable. The shape-shifting behaviors considered in 4D printing include folding, bending, twisting, linear or nonlinear expansion/contraction, surface curling, and generating surface topographical features. The shapes can shift from 1D to 1D, 1D to 2D, 2D to 2D, 1D to 3D, 2D to 3D, and 3D to 3D. In the 4D printing auxetic structure, the kinetiX is a cellular-based material design composed of rigid plates and elastic hinges. In pneumatic auxetics based on the kirigami structure, an inverse optimization method for designing and fabricating morphs three-dimensional shapes out of patterns laid out flat. When 4D printing material is molded into a deformable 3D structure, it can be applied to the exoskeleton material of soft robots such as upper and lower limbs, fingers, hands, toes, and feet. Research on 4D printing materials for soft robots is essential in developing smart clothing for healthcare in the textile and fashion industry.

• Journal of The Korean Digital Architecture Interior Association
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• v.9 no.3
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• pp.85-93
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• 2009

In this study, the ex-formal expressions observed in space form of Korean modern architecture are distributed for characteristic analysis based on the period and type. The result of the study is certified by the work analysis and the result is as follows. Initially, due to the limited materials and influence of western brutalism, the works developed during 1960~70 tend to be plastic and contain expressionism. Around 1980's, the works tend to show forms of amusement and popularity. In 1990's the works show significance in deconstructive expression. From after 2000, ecological concept of architecture was introduced and organic expression started increasing Secondly, the ex-formal expressions are found to be in four different types. The organic expression is shown regardless of the period. In modern days, not only the physical properties of materials, but also the ecological concept is combined with the organic expression and is in increase. The plural expression started appearing after the 1980's and the sculptural diversity is enhancing with the addition of decorative factors or modification of geometrical form. The ex-construction and deconstructive expression show significance in some characteristics such as folding, inclination, and geometrical explosion. The free form and nonlinear expression tend to increase dramatically based on the development of structure technology as well as execution and introduce of the digital design technique.

• Bulletin of the Korean Chemical Society
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• v.22 no.8
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• pp.872-876
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• 2001

Topological changes caused by the alkaline and enzymatic attacks of solution-grown, chain-folded lamellar crystals (SGCs) of poly[(R)-3-hydroxybutyrate] P(3HB) have been studied in order to investigate the chain-folding structure in P(3HB) crystal regions. NaOH and an extracellular PHB depolymerase purified from Alcaligenes faecalis T1 were used for alkaline and enzymatic hydrolysis, respectively. The measurements were performed on crystals attached to a substrate which is inactive to degradation mediums. Both alkaline and enzymatic attacks lead to a breakup of the lamellar crystals along the crystallographic b-axis during initial erosion. Since hydrolysis preferentially occurs in amorphous regions, this morphological result reflects relatively loosely packed chains in core parts of lamellar crystals. Additionally, it was supported by the ridge formation along the b-axis in the lamellar crystals after thermal treatment at a low temperature because of the thermally sensitive nature of the loosely packed chains in lamellar crystals. However, the alkaline hydrolysis accompanied the chain erosions or scissions in quasi-regular folded lamellar surfaces due to smaller size of alkaline ions in comparison to the enzyme, resulting in the decrease of molecular weight.

• Biotechnology and Bioprocess Engineering:BBE
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• v.7 no.3
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• pp.155-162
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• 2002

The cyclic amidohydrolase family enzymes, which include allantoinase, dihydroorotase, dihydropyrimidinase and (phenyl)hydantoinase, are metal-dependent hydrolases and play a crucial role in the metabolism of purine and pyrimidine in vivo. Each enzyme has been independently characterized, and thus well documented, but studies on the higher structural traits shared by members of this enzyme family are rare due to the lack of comparative study. Here, we report upon the expression in E. coli cells of maltose-binding protein (MBP)- and glutathione S-transferase (GST)-fused cyclic amidohydrolase family enzymes, facilitating also for both simple purification and high-level expression. Interestingly, the native quaternary structure of each enzyme was maintained even when fused with MBP and GST. We also found that in fusion proteins the favorable biochemical properties of family enzymes such as, their optimal pHs, specific activities and kinetic properties were conserved compared to the native enzymes. In addition, MBP-fused enzymes showed remarkable folding ability in-vitro. Our findings, therefore, suggest that a previously unrecognized trait of this family, namely the ability to functional fusion with some other protein but yet to retain innate properties, is conserved. We described here the structural and evolutionary implications of the properties in this family enzyme.

• Molecules and Cells
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• v.25 no.4
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• pp.494-503
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• 2008

Many therapeutic glycoproteins have been successfully generated in plants. Plants have advantages regarding practical and economic concerns, and safety of protein production over other existing systems. However, plants are not ideal expression systems for the production of biopharmaceutical proteins, due to the fact that they are incapable of the authentic human N-glycosylation process. The majority of therapeutic proteins are glycoproteins which harbor N-glycans, which are often essential for their stability, folding, and biological activity. Thus, several glyco-engineering strategies have emerged for the tailor-making of N-glycosylation in plants, including glycoprotein subcellular targeting, the inhibition of plant specific glycosyltranferases, or the addition of human specific glycosyltransferases. This article focuses on plant N-glycosylation structure, glycosylation variation in plant cell, plant expression system of glycoproteins, and impact of glycosylation on immunological function. Furthermore, plant glyco-engineering techniques currently being developed to overcome the limitations of plant expression systems in the production of therapeutic glycoproteins will be discussed in this review.

• BMB Reports
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• v.44 no.10
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• pp.653-658
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• 2011

Sclerotinia sclerotiorum fungus has three endoxylanases induced by wheat bran. In the first part, a partial xylanase sequence gene (90 bp) was isolated by PCR corresponding to catalytic domains (${\beta}5$ and ${\beta}6$ strands of this protein). The high homology of this sequence with xylanase of Botryotinia fuckeliana has permitted in the second part to amplify the XYN1 gene. Sequence analysis of DNA and cDNA revealed an ORF of 746 bp interrupted by a 65 bp intron, thus encoding a predicted protein of 226 amino acids. The mature enzyme (20.06 kDa), is coded by 188 amino acid (pI 9.26). XYN1 belongs to G/11 glycosyl hydrolases family with a conserved catalytic domain containing $E_{86}$ and $E_{178}$ residues. Bioinformatics analysis revealed that there was no Asn-X-Ser/Thr motif required for N-linked glycosylation in the deduced sequence however, five O-glycosylation sites could intervene in the different folding of xylanses isoforms and in their secretary pathway.