• Transactions of the Korean Society of Mechanical Engineers A
• /
• v.34 no.9
• /
• pp.1235-1240
• /
• 2010

Wire-woven Bulk Kagome (WBK) is fabricated by assembling helically formed wires in six directions. To date, WBK samples have been assembled manually. For industrial application, the assembly process must be automated. Furthermore, if WBK is to be fabricated using flexible wires that cannot maintain their helical shape during fabrication, a specialized automatic machine, i.e., a loom needs to be developed. In this work, we designed and constructed a loom for fabricating WBKs using flexible wires. This loom is operated by one rotation of the upper plate, two translations of the insertion device, and insertion of wires. So-called "comb devices" are placed between multiple layers of Kagome nets to prevent the wires that are already in place from getting entangled with those that are being inserted. This loom can be also used to fabricate semi-WBKs composed of helically formed wires and rigid straight wires.

• Composites Research
• /
• v.30 no.6
• /
• pp.331-337
• /
• 2017

The composite lattice structures have advantages of high specific stiffness and strength and are mainly applied to the structures of launch vehicles that carry the compressive load. However, since these structures are manufactured by filament winding technology, there are some defects and voids found in the knots. For these reasons, the stiffness and strength of the lattice structures have to be compared with finite element model for predicting design load. But, the full scale test is difficult because time and space are limited and the shape of structure is complex, and hence the simple and reliable test methods for examination of stiffness are needed. In this paper, subelements of composite lattice structures were prepared and compressive and bending test were conducted for examination of stiffness of helical and hoop rib. Test methods for subelements of composite lattice structures that has curved and twisted shape were supposed and compared with finite element analysis results.

• Fisheries and Aquatic Sciences
• /
• v.12 no.1
• /
• pp.6-15
• /
• 2009

Biochemical and functional properties of acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from rockfish skin were characterized. Yield of PSC (90.0%) was higher than that of ASC (63.2%). Both ASC and the PSC consisted of ${\alpha}1$ and ${\alpha}2$ chains, and $\alpha$-cross-linked components. According to the results of hydroxylation of proline and lysine, and FT-IR, no difference between the helical structure of ASC and PSC was identified. Thermal denaturation temperature (TDT) of ASC from rockfish skin was $22.8^{\circ}C$, the same as exhibited in PSC. Both ASC and PSC were higher in water absorption capacity (WAC) and oil absorption capacity (OAC) than other vegetable proteins. According to the results of emulsifying activity (EA) and cooking stability (CS), both ASC and PSC from rockfish skin were inferior compared to the commercial emulsifier (Tween-80). The results of FT-IR suggested that the structure of PSC was slightly different when compared to that of ASC. No differences in solubility were established between ASC and PSC from rockfish skin at various pH and NaCl concentrations.

• Proceedings of the Korean Biophysical Society Conference
• /
• 2003.06a
• /
• pp.75-75
• /
• 2003

We report here the results on N-acetyl-N'-dimethylamide of proline (Ac-Pro-NM $e_2$) calculated using the ab initio molecular orbital method with the self-consistent reaction field (SCRF) theory at the HF level with the 6-31+G(d) basis set to investigate the conformational preference of polyproline depending on the cis/trans peptide bonds and down/up puckerings along the backbone torsion angle $\square$ in the gas phase, chloroform, and water. In the gas phase, Ac-Pro-NM $e_2$ has seven local minima of tFd, tFu, cFd, cFu, cAu, tAu, and cAd conformations. In particular, polyproline conformations tFd, tFu, cFd, and cFu are found to be more stable than $\square$-helical conformations cAu, tAu, and cAd. In contrast, Ac-Pro-NHMe has seven local minima of tCd, tCu, cBd, cAu, tAu, cFd, and cFu conformations. Conformations tCd and tCu are found to be most stable, which is ascribed to the intramolecular hydrogen bond between C=O of acetyl group and $N^{~}$ H of N'-methyl amide group. The stability of the cFd conformation (i.e., the polyproline I structure) in chloroform is somewhat increased, relative to that in water, although tFd and tFu conformations (i.e., the polyproline II structure) are dominate both in chloroform and water. The population of backbone conformations feasible in chloroform and water is consistent with the experiments. This work is supported by a Korea Research Foundation Grant (KRF-2002-041-C00129).

• Proceedings of the Korean Biophysical Society Conference
• /
• 2003.06a
• /
• pp.69-69
• /
• 2003

Human CD99 is a ubiquitous 32-kDa transmembrane protein encoded by the mic2 gene. The major cellular functions of CD99 protein are related to homotypic cell adhension, apoptosis, vesicular protein transport, and differentiation of thymocytes or T cells. Recently it has been reported that expression of a splice variant of CD99 transmembrane protein (Type I and Type II) increases invasive ability of human breast cancer cells. To understand structural basis for cellular functions of CD99 (Type I), we have initiated studies on hCD99$^{TMcytoI}$ and hCD99$^{cytoI}$ using circular dichroism (CD) and multi-dimensional NMR spectroscopy. CD spectrum of hCD99$^{TMcytoI}$ in the presence of 200mM DPC and CHAPS displayed an existence $\alpha$-helical conformation. The solution structure of hCD99$^{cytoI}$ determined by NMR is composed of one N-terminal $\alpha$-helix, $\alpha$A, two C-terminal short $\alpha$-helix segments, $\alpha$B and $\alpha$C. While $\alpha$A and $\alpha$B are connected by the long flexible loop, $\alpha$B and $\alpha$C connected by type III$\beta$-turn. Although it has been rarely figured out the correlation between structure and functional mechanism of hCD99$^{TMcytoI}$ and hCD99$^{cytoI}$, there is possibility of dimerization or oligomerization. In addition, the feasible mechanism of hCD99$^{cytoI}$ is that it could have intramolecular interaction between the N- and C- terminal domain through large flexible AB loop.

• Molecules and Cells
• /
• v.38 no.8
• /
• pp.715-722
• /
• 2015

In Gram-negative bacteria in the periplasmic space, the dimeric thioredoxin-fold protein DsbC isomerizes and reduces incorrect disulfide bonds of unfolded proteins, while the monomeric thioredoxin-fold protein DsbA introduces disulfide bonds in folding proteins. In the Gram-negative bacteria Salmonella enterica serovar Typhimurium, the reduced form of CueP scavenges the production of hydroxyl radicals in the copper-mediated Fenton reaction, and DsbC is responsible for keeping CueP in the reduced, active form. Some DsbA proteins fulfill the functions of DsbCs, which are not present in Gram-positive bacteria. In this study, we identified a DsbA homologous protein (CdDsbA) in the Corynebacterium diphtheriae genome and determined its crystal structure in the reduced condition at $1.5{\AA}$ resolution. CdDsbA consists of a monomeric thioredoxin-like fold with an inserted helical domain and unique N-terminal extended region. We confirmed that CdDsbA has disulfide bond somerase/reductase activity, and we present evidence that the N-terminal extended region is not required for this activity and folding of the core DsbA-like domain. Furthermore, we found that CdDsbA could reduce CueP from C. diphtheriae.

• Journal of the Korean Magnetic Resonance Society
• /
• v.9 no.2
• /
• pp.110-121
• /
• 2005

E.coli methionyl tRNA synthetase consist of 676 amino acids and plays a key role in initiation of protein synthesis. The native form of this enzyme is a homodimer, but the monomeric enzyme truncated approximately C-terminal 120 amino acids retains the full enzymatic activities. X-ray crystal structure of the active monomeric enzyme shows that it has two domains. The N-terminal domain is thought to be a binding site for acceptor stem of tRNA, ATP, and methionine. The C-terminal domain is mainly a-helical and makes an interaction with the anticodon of $tRNA^{Met}$. Especially it is suggested that the region of helix-loop-helix including the tryptophan residue at the position 461 may be the essential for the interaction with anticodon of $tRNA^{Met}$. In this work the structure and function of E. coli methionyl-tRNA synthetase was studied by spectroscopic method (NMR, CD, Fluorescence). The importance of tryptophan residue at the position 461 was investigated by fluorescence spectroscopy. Tryptophan 461 is expected to be an essential site for the interaction between E. coli methionyl-tRNA synthetase and E. coli $tRNA^{Met}$. Proton and heteonuclear 2-dimensional NMR spectroscopy were also used to elucidate the protein-tRNA interaction.

• Korean Journal Plant Pathology
• /
• v.2 no.1
• /
• pp.1-11
• /
• 1986

Negatively stained dip preparations from Euonymus showing vein clear symptoms revealed bacilliform particles. The particles tentatively referred to as the Euonymus vein clear virus(EVCV) have a relatively complex structure, measuring 230-280nm in length and 70-80nm in diameter. They have an envelope, 8-10nm thick, provided with evenly spaced beadlike projection about 5-6nm long. The inner tubular core which had no envelope showed helical structures, 200-220nm long, and 50-55nm in diameter. This inner tubular core is interpreted as the virus nucleocapsid. A striking association of virus particles with the nuclei of infected cells was apparent from sections which showed numberous virus particles at the nuclear periphery and in what appeared to be intranuclear virus particle inclusions. Careful examination of these apparent inclusions revealed the presence of the nuclear envelope surrounding them, in addition to cytoplasmic organelles within them. Such profiles were interpreted as having arisen when the sections passed through invaginations of the cytoplasm into the nucleus. In all the sections showing virus particles associated with the nucleus, large number of virus particles were found to be present in expanded areas between the two lamellae of the nuclear envelope. This location is suggested as a possible site of virus assembly. Serveal micrographs of particles found in this location suggested incorporation of the inner lamella of the nuclear envelope into the viral envelope. Various micrographs indicated a possible helical arrangement of certain components present in the virus core.

• Polymer(Korea)
• /
• v.33 no.3
• /
• pp.254-262
• /
• 2009

Nine kinds of hydroxypropyl celluloses (HPCs) with degree of substitution (DS) and molar substitution (MS) ranging from 2.10 to 2.71 and 2.3 to 6.7, respectively and seven kinds of fully butanoated HPCs (BPCs) based on the HPCs with $2.3\;{\le}\;MS\;{\le}\;6.7$ were synthesized, and the molecular characteristics of HPCs and the thermotropic liquid crystalline properties of the derivatives were investigated. MS was nearly equal to DS for small value of DS, but it became exceedly larger than DS for $DS{\gtrsim}1$, showing that in the later stages of reaction, propylene oxide preferentially adds to the side chains rather than the main chain. All the derivatives formed enantiotropic cholesteric phases with right-handed helical structures. The glass and clearing transition temperatures of both HPCs and BPCs were decreased with increasing MS. The optical pitches (${\lambda}_m'S$) of BPCs, as well as HPCs themselves, increased with increasing temperature. However, the ${\lambda}_m'S$ of both HPCs and BPCs at the same temperature increased with increasing MS. Moreover, the temperature dependence of ${\lambda}_m$ of HPCs was weaker than that of BPCs, suggesting that the helical twisting power of the cellulose chain highly depends on the length and chemical structure of the side chain introduced in cellulose chain.

• Polymer(Korea)
• /
• v.33 no.2
• /
• pp.144-152
• /
• 2009

The thermal and optical properties of poly {1-(cholesteryloxycarbonylalkanoyloxy) ethylene}s (PCALEn, n=2$\sim$8,10, the number of methylene units in the spacer) were investigated. All of the homologues formed monotropic cholesteric phases with left-handed helical structures. PCALEn with n=2 or 10, in constrast with PCALEn with $3{\leq}n{\leq}8$, did not display reflection colors over the full cholesteric range, suggesting that the helical twisting power of the cholesteryl group highly depends on the length of the spacer connecting the cholesteryl group to the polyethylene chain. The glass transition temperatures decreased with increasing n. The isotropic-cholesteric phase transition temperatures decreased with increasing n up to 7 and showed an odd-even effect. However it became almost constant when n is more than 7. This behavior is rationalized in terms of the change in the average shape of the side chain on varing the parity of the spacer. This rationalization also accounts for the observed variation of the entropy gain for the clearing transition. The thermal stability and degree of order in the mesophase and the temperature dependence of the optical pitch observed for PCALEn were significantly different from those reported for cellulose tri(cholesteryloxycarbonyl)alkanoates. The results were discussed in terms of the differences in the chemical structure and flexibility of main chain and the number of the mesogenic units per repeating unit.