２０００年代におけるフィルム・コミッション論の検証

departmental bulletin pape

Piezoelectric Strain Control of Terahertz Spin Current

Electrical control of photogenerated terahertz (THz) spin current pulses from a spintronic emitter has been at the forefront for the development of scalable, cost-efficient, wideband optospintronic devices. Artificially combined ferroelectric and ferromagnet heterostructure provides the potential avenue to deterministically control the phase of THz spin current pulse through piezoelectric strain. Here, the electric field-mediated piezoelectric strain control of photogenerated THz spin current pulse from a multiferroic spintronic emitter is demonstrated. The phase reversal of the THz spin current pulse is obtained from the combined effect of piezoelectric strain and a small magnetic field applied opposite to the initial magnetization of the ferromagnet. The piezoelectric strain-controlled phase switching of THz spin current thus opens a door to develop efficient strain engineered scalable on-chip THz spintronics devices.journal articl

Production of Prompt Charmonia in e+e- Annihilation at sqrt[s] ≈ 10.6 GeV

journal articl

ヒョウメン シンブッシツ ソウセイ ト ナノバイオサイエンス

video/mp4講演者所属: 大阪大学産業科学研究所高次制御材料科学大部門教授vide

Lipoxygenase-catalyzed polymerization of phenolic lipids suggests a new mechanism for allergic contact dermatitis induced by urushiol and its analogs

journal articl

The evolving 3D model of dimer Super Mini-B (dimer S-MB) in SDS/water at the starting (“0 nsec”) and ending (“10 nsec”) times of the MD simulation.

<p><u>Plate A</u>: Snapshot of dimer S-MB at “0 nsec” (see text). DSSP analysis indicated helical regions (residues in parentheses) for S-MB molecules <i>A</i> (14–17, 30–37) and <i>B</i> (14–18, 31–39). The local 2-fold axis relating the two monomers in the dimer is shown by an arrow. <u>Plate B</u>: Snapshot of S-MB at “10 nsec”. DSSP analysis indicated helical regions for S-MB molecules <i>A</i> (8–10, 17–21, 30–37) and <i>B</i> (11–16, 31–38). In Plates A and B, MD simulations were performed in the GROMACS version 3.3.3 environment (see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0008672#s2" target="_blank"><u>Methods</u></a>). The protein backbone structure is shown with color-coded ribbons denoting the following domains: N-terminal insertion sequence (green), N-terminal helix (red), turn-loop (green), and C-terminal helix (red) rendered with Rasmol 2.7.4.2. Appropriately colored side-chains are shown as stick figures attached to the N-terminal insertion sequence (green), helix (red) or loop (green) ribbon backbones. Disulfide linkages between the N-terminal helix in the foreground and C-terminal helix in the background are highlighted in yellow. The helices are predominately α-helical, with additional minor contributions from 3₁₀ - and 5-helices. The side-chains and backbones for the two N-terminal phenylalanines are colored purple. The N-terminal sequences (residues 1–7) adopt extended conformations that are centered just over the N- and C-terminal helices, with each having its N-terminal Phe-1 near the loop region (Gly-25 and Gly-26). The 30 bound SDS detergent molecules are shown as wireframe molecules that are colored according to the cpk convention. The “0 nsec” dimer S-MB structure in Plate A is similar to the initial ZDOCK and Rosetta input structures (see text).</p

Surface activity of DEPN-8+1.5% (by wt) Mini-B and CLSE in the presence of bovine serum albumin.

<p>Surface tension at minimum radius (minimum surface tension) is graphed as a function of time for DEPN-8+1.5% Mini-B and CLSE in the presence of bovine serum albumin (3 mg/ml) on a pulsating bubble surfactometer (37°C, 20 cycles/min, 50% area compression). Surfactant concentration was 2.5 mg/ml of phosphonolipid (phospholipid). Data are Mean±SEM for n = 4–5.</p

Quasi-static surface activity of DEPN-8+1.5% or 3% Mini-B compared to CLSE on the captive bubble surfactometer.

<p>Minimum and maximum surface tensions are shown for DEPN-8+1.5% or 3% by weight Mini-B compared to CLSE on a captive bubble surfactometer during slow compression (10 cycles over 90 min including a 2 min pause between each cycle). Surface tension values are Mean±SEM for at least three separate experiments. See text for details.</p

Spectroscopic behavior of Mini-B and DEPN-8.

<p><u>Panel A</u>: CD spectrum for Mini-B in trifluoroethanol (TFE); <u>Panel B</u>: FTIR spectrum for DEPN-8; <u>Panel C</u>: FTIR spectral differences for Mini-B in DEPN-8 (dashed line) compared to Mini-B in TFE (solid line). In Panel A, mean residue ellipticity (MRE) averaged over eight scans is plotted against wavelength for Mini-B in 4∶6 (v:v) TFE:10 mM phosphate buffer, pH 7.4. The double minimum at ∼208 and 222 nm is indicative of a high α-helical content. In Panel B, the spectrum for DEPN-8 multilayers (100 µg lipid, arbitrary absorbance units) has a “C-O-C” ether linkage-associated absorption band centered at a wavenumber of 1072 cm⁻¹. In Panel C, the IR spectrum of Mini-B in TFE (solid line) has a peak at 1655 cm⁻¹ indicating high α-helix levels, while the peak at 1658 cm⁻¹ and high-field shoulder at 1678 cm⁻¹ for Mini-B in DEPN-8 (dashed line) indicates an increase in turn/bend conformation with a decreased but still prominent α-helix content. See text for discussion.</p

Conformational drift indicated as α-C root mean square deviation (RMSD) from the starting structure for the MD simulation of the monomeric MB and S-MB peptides.

<p><u>Plate A</u>: Time course of the RMSD in nm from the “0 nsec” structure of MB (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0008672#pone-0008672-g004" target="_blank">Fig. 4A</a>). <u>Plate B</u>: Time course of the RMSD from the “0 nsec” structure of S-MB (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0008672#pone-0008672-g007" target="_blank">Fig. 7A</a>). See <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0008672#s2" target="_blank"><u>Methods</u></a> for experimental details.</p