• Title/Summary/Keyword: isothermal

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Pass Design of Drawing Process to Prevent Delamination (층간분리 방지를 위한 인발공정 패스설계)

  • Lee, S.K.;Ko, D.C.;Kim, B.M.
    • Proceedings of the Korean Society for Technology of Plasticity Conference
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    • 2008.10a
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    • pp.46-49
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    • 2008
  • Drawing process of the high carbon steel wire with high speed is usually performed at room temperature using multi pass. Tn the multi pass drawing, temperature rise affects the mechanical properties of the final product. The excessive temperature rise during the deformation promotes the occurrence of delamination, and deteriorates the torsion property and durability of wire. This paper investigates the occurrence of delamination in the wire through the torsion test and the evaluation of wire temperature. The excessive wire temperature ieads to the occurrence of delamination. Based on the calculation of the wire temperature, a new pass schedule, that can prevent the delamination due to the excessive wire temperature rise, is designed through the isothermal pass schedule.

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Engineering and Characterization of the Isolated C-Terminal Domain of 5-Enolpyruvylshikimate-3-phosphate (EPSP) Synthase

  • Kim, Hak-Jun;Kim, Hyun-Woo;Kang, Sung-Ho
    • Journal of Microbiology and Biotechnology
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    • v.17 no.8
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    • pp.1385-1389
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    • 2007
  • 5-Enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the formation of EPSP and inorganic phosphate from shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) in the biosynthesis of aromatic amino acids. To delineate the domain-specific function, we successfully isolated the discontinuous C-terminal domain (residues 1-21, linkers, 240-427) of EPSP synthase (427 residues) by site-directed mutagenesis. The engineered C-terminal domains containing no linker (CTD), or with gly-gly ($CTD^{GG}$) and gly-ser-ser-gly ($CTD^{GSSG}$) linkers were purified and characterized as having distinct native-like secondary and tertiary structures. However, isothermal titration calorimetry (ITC), $^{15}N-HSQC$,\;and\;^{31}P-NMR$ revealed that neither its substrate nor inhibitor binds the isolated domain. The isolated domain maintained structural integrity, but did not function as the half of the full-length protein.