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      • KCI등재

        Application of Different Diffraction Peak Profile Analysis Methods to Study the Structure Evolution of Cold-Rolled Hexagonal α-Titanium

        Ivan V. Ivanov,Daria V. Lazurenko,Andreas Stark,Florian Pyczak,Alexander Thömmes,Ivan A. Bataev 대한금속·재료학회 2020 METALS AND MATERIALS International Vol.26 No.1

        This paper presents a comparison between the “classical” and the modified Williamson–Hall and Warren–Averabach methodsapplied to an analysis of the microstructure of -titanium. The microstructural parameters of cold-rolled titanium specimenswere retrieved from analysis of the X-ray diffraction (XRD) peaks. The high-quality XRD patterns were received at the P07beamline (The High Energy Materials Science) at the German electron synchrotron. The dependence of the crystallite size,the inhomogeneous microstrains, the average dislocation density, the dislocation cut-off radius and some other parameterson the plastic strain were estimated. The results clearly indicate that, due to the consideration of the dislocation contrasteffect, the modified models are a much better fit to the experimental data in comparison with the “classical” models. Theresults of hardness and corrosion resistance measurements of Ti samples can be explained based on the results obtainedfrom the XRD analysis.

      • Autodisplay of streptavidin

        Park, Min,Jose, Joachim,Thö,mmes, Sarah,Kim, Jo-Il,Kang, Min-Jung,Pyun, Jae-Chul Elsevier 2011 Enzyme and microbial technology Vol.48 No.4

        <P><B>Abstract</B></P><P>Streptavidin was expressed on the outer membrane of <I>E. coli</I> as a recombinant fusion protein with an autotransporter domain called AIDA-I (adhesin involved in diffuse adherence) using autodisplay technology. The autodisplay of streptavidin was confirmed by SDS-PAGE of the outer membrane proteins, and the number of autodisplayed streptavidin molecules on a single <I>E. coli</I> cell was evaluated with densitometric analysis. The biotin-binding activity of the autodisplayed streptavidin was estimated after treatment with fluorescently labeled biotin by fluorescence microscopy and flow cytometry. The biotin-binding activity of the <I>E. coli</I> with autodisplayed streptavidin was compared with the activity of streptavidin immobilized on magnetic beads. Finally, the outer membrane presenting autodisplayed streptavidin was isolated and layered on a 96-well microplate for an immunoassay.</P>

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