• Mycobiology
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• v.43 no.3
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• pp.272-279
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• 2015

To screen molecular chaperones similar to small heat shock proteins (sHsps), but without ${\alpha}$-crystalline domain, heat-stable proteins from Schizosaccharomyces pombe were analyzed by 2-dimensional electrophoresis and matrix assisted laser desorption/ionization time-of-flight mass spectrometry. Sixteen proteins were identified, and four recombinant proteins, including cofilin, NTF2, pyridoxin biosynthesis protein (Snz1) and Wos2 that has an ${\alpha}$-crystalline domain, were purified. Among these proteins, only Snz1 showed the anti-aggregation activity against thermal denaturation of citrate synthase. However, pre-heating of NTF2 and Wos2 at $70^{\circ}C$ for 30 min, efficiently prevented thermal aggregation of citrate synthase. These results indicate that Snz1 and NTF2 possess molecular chaperone activity similar to sHsps, even though there is no ${\alpha}$-crystalline domain in their sequences.

• Fibers and Polymers
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• v.3 no.1
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• pp.18-23
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• 2002

The structure development and dynamic properties of fibers produced by high-speed spinning of P(EN-ET) random copolymers were investigated. The as-spun fibers were found to remain amorphous up to the spinning speed of 1500 m/min, and subsequent increases in speed resulted in the crystalline domains containing primarily $\alpha$ crystalline modification of PEN. The f modification was not found up to spinning speeds of 4500 m/min. On the other hand, annealing of constrained fibers spun at the 2100 m/min at 180,200, and 240^{\circ}C$ exhibited $\beta$-form crystalline structure, while the annealed fibers spun in 600-1500 m/min range exhibited dominantly $\alpha$-form. However $\beta$-form crystals disappeared above the spinning speed of 3000 m/min. With increasing spinning speeds from 600 to 4500 m/min, the storage modulus of as-spun fibers increased continuously and reached a value of about 10.4 spa at room temperature. The tan $\delta$curves showed the $\alpha$-relaxation peak at about 155-165^{\circ}C$, which is considered to correspond to the glass transition. The $\alpha$-relaxation peaks became smaller and broader, and shift to higher temperatures as the spinning speed increases, meaning that molecular mobility in the amorphous region is restricted by increased crystalline domain.

• Journal of Magnetics
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• v.7 no.2
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• pp.51-54
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• 2002

The crystallization of amorphous Ba-ferrite/sapphire(001) thin films was studied in real-time synchrotron x-ray scattering experiments. In the sputter-grown amorphous films, we found the existence of epitaxial $Fe_3O_4$ interfacial crystallites (50-${\AA}$-thick), well aligned $[0.03^circ$full-width at half-maximum (FWHM)] to the sapphire [001] direction. The amorphous precursor was crystallized to epitaxial Ba-ferrite and \alpha-Fe_2O_3$grains in two steps; i) the nucleation of crystalline \alpha-Fe_2O_3$ phase started at $300^circ{C}$ together with the transformation of the $Fe_3O_4$ crystallites to the \alpha-Fe_2O_3$ crystallites, ii) the nucleation of Ba-ferrite phase occurred at temperature above $600^circ{C}$. In the crystallized films irrespective of the film thickness, the crystal domain size of the \alpha-Fe_2O_3$grains was about 250 ${\AA}$ in the film plane, similar to that of the Ba-ferrite grains.

• The Korean Journal of Ceramics
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• v.2 no.3
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• pp.152-156
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• 1996

Fine (~0.09 $\mu$m) $\beta$-SiC Powders with 3.3wt% of large (~0.44$\mu$m) $\alpha$-SiC of $\beta$-SiC particles (seeds) added were hotpressed at 175$0^{\circ}C$ using $Y_2O_3$, $Al_2O_3$ and CaO as sintering aids and then annealed at 185$0^{\circ}C$ for 4 h to enhance grain growth. The resultant microstructure and polytypes were analyzed by high resolution electron microscopy (HREM).Growth of $\beta$-SiC with high density of microtwins and formation of ${\alpha}/{\beta}$ composite grains consisting of $\alpha$-SiC domain sandwiched between $\beta$-SiC domains were found in both specimens. When large $\alpha$-SiC (mostly 6H) seeds were added, the $\beta$-SiC transformend preferentially to the 6H polytype. In contrast, when large $\beta$-SiC (3C) seeds were added, the fine $\beta$-SiC transformed preferentially to the 4H polytype. Such results suggested that the polytype formation in SiC was influenced by crystalline form of seeds added as well as the chemistry of sintering aids. The ${\alpha}/{\beta}$ interface played and important role in the formation of elongated grains as evidenced by presence of ${\alpha}/{\beta}$ composite grains with high aspect ratio.

• Asian-Australasian Journal of Animal Sciences
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• v.29 no.1
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• pp.126-133
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• 2016

A gene from Actinomyces sp. Korean native goat (KNG) 40 that encodes an endo-${\beta}$-1,4-glucanase, EG1, was cloned and expressed in Escherichia coli (E. coli) $DH5{\alpha}$. Recombinant plasmid DNA from a positive clone with a 3.2 kb insert hydrolyzing carboxyl methyl-cellulose (CMC) was designated as pDS3. The entire nucleotide sequence was determined, and an open-reading frame (ORF) was deduced. The ORF encodes a polypeptide of 684 amino acids. The recombinant EG1 produced in E. coli $DH5{\alpha}$ harboring pDS3 was purified in one step using affinity chromatography on crystalline cellulose and characterized. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis/zymogram analysis of the purified enzyme revealed two protein bands of 57.1 and 54.1 kDa. The amino terminal sequences of these two bands matched those of the deduced ones, starting from residue 166 and 208, respectively. Putative signal sequences, a Shine.Dalgarno-type ribosomal binding site, and promoter sequences related to the consensus sequences were deduced. EG1 has a typical tripartite structure of cellulase, a catalytic domain, a serine-rich linker region, and a cellulose-binding domain. The optimal temperature for the activity of the purified enzyme was $55^{\circ}C$, but it retained over 90% of maximum activity in a broad temperature range ($40^{\circ}C$ to $60^{\circ}C$). The optimal pH for the enzyme activity was 6.0. Kinetic parameters, $K_m$ and $V_{max}$ of rEG1 were 0.39% CMC and 143 U/mg, respectively.