Seoul, South Korea
Seoul, South Korea

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Choi J.,Creative Research Center | Lee C.-B.,Dongseo University | Kim H.-T.,Creative Research Center | Kim H.-T.,Korean University of Science and Technology
Journal of Magnetism and Magnetic Materials | Year: 2012

In order to find evidence of the ferromagnetic interaction, the crystal structure and the magnetic property of pure Fe are investigated from room temperature to 950 °C by measuring X-ray diffraction patterns and magnetizations. The ferro-paramagnetic transition occurs near 770 °C with large stretch and contraction of lattice constants, which is an evidence of correlation of ferromagnetism and crystal structure. The structural phase transition between α-bcc and γ-fcc is observed above 850 °C. The d-spaces between (011) and (101) planes, observed with a high resolution triple-axis X-ray diffractometer, differ at RT; Δd≡d 101-d 011≈0.45%. The structure of Fe is pseudocubic, showing a body-centered tetragonal structure of c/a<1 generated by magnetostriction (exchange striction) induced by spontaneous magnetization. © 2012 Elsevier B.V.

Yeom K.-H.,Seoul National University | Yeom K.-H.,Technical University of Delft | Heo I.,Seoul National University | Lee J.,Creative Research Center | And 4 more authors.
EMBO Reports | Year: 2011

Single-molecule techniques have been used for only a subset of biological problems because of difficulties in studying proteins that require cofactors or post-translational modifications. Here, we present a new method integrating single-molecule fluorescence microscopy and immunopurification to study protein complexes. We used this method to investigate Lin28-mediated microRNA uridylation by TUT4 (terminal uridylyl transferase 4, polyU polymerase), which regulates let-7 microRNA biogenesis. Our real-time analysis of the uridylation by the TUT4 immunoprecipitates suggests that Lin28 functions as a processivity factor of TUT4. Our new technique, SIMPlex (single-molecule approach to immunoprecipitated protein complexes), provides a universal tool to analyse complex proteins at the single-molecule level. © 2011 European molecular biology organization.

Kyung K.-U.,Creative Research Center | Lee J.-Y.,Smart Interface Team | Park J.,Smart Interface Team | Srinivasan M.A.,Massachusetts Institute of Technology
Presence: Teleoperators and Virtual Environments | Year: 2012

In this work, we designed an interactive stylus interface for touch-screen devices, the wUbi-Pen haptic stylus. The stylus has functions of providing both vibration and impact with a single actuator, and it is a stand-alone system including its own battery and communication module. We present a new interaction scheme on the graphical user interface (GUI) based on sensory feedback events for clicking, drag-and-drop, moving, sliding, highlighting, and drawing. Experiments evaluating stylus performance indicated that the haptic cues improved precise control of GUI elements. A simple interactive digital sketchbook was also implemented, which provided a variety of haptic feedback while drawing and touching objects. © 2012 by the Massachusetts Institute of Technology.

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