Localized Distributions of Quasi Two-Dimensional Electronic States near Defects Artificially Created at Graphite Surfaces in Magnetic Fields

We measured the local density of states of a quasi two-dimensional electron system (2DES) near defects, artificially created by Ar-ion sputtering, on surfaces of highly oriented pyrolytic graphite (HOPG) with scanning tunneling spectroscopy (STS) in high magnetic fields. At valley energies of the Landau level spectrum, we found two typical localized distributions of the 2DES depending on the defects. These are new types of distributions which are not observed in the previous STS work at the HOPG surface near a point defect [Y. Niimi \textit{et al}., Phys. Rev. Lett. {\bf 97}, 236804 (2006).]. With increasing energy, we observed gradual transformation from the localized distributions to the extended ones as expected for the integer quantum Hall state. We show that the defect potential depth is responsible for the two localized distributions from comparison with theoretical calculations.Comment: 4 pages, 3 figure

Single grain (LRE)-Ba-Cu-O superconductors fabricated by top seeded melt growth in air

We have recently reported a practical processing method for the fabrication in air of large, single grain (LRE)-Ba-Cu-O [where LRE Nd, Sm, Eu and Gd] bulk superconductors that exhibit high Tc and high Jc. The process is based initially on the development of a new type of generic seed crystal that can promote effectively the epitaxial nucleation of any (RE)-Ba-Cu-O system and, secondly, by suppressing the formation of (LRE)/Ba solid solution in a controlled manner within large LRE-Ba-Cu-O grains processed in air. In this paper we investigate the degree of homogeneity of large grain Sm-Ba-Cu-O superconductors fabricated by this novel process. The technique offers a significant degree of freedom in terms of processing parameters and reproducibility in the growth of oriented single grains in air and yields bulk samples with significantly improved superconducting and field-trapping properties compared to those processed by conventional top seeded melt growth (TSMG)

Myosin IX: A Single-Headed Processive Motor

The class IX myosin is a member of the myosin superfamily and found in variety of tissues. Myosin IX is quite unique among the myosin superfamily in that the tail region contains a GTPase activating protein (GAP) domain for the small GTP-binding protein, Rho. Recently it was reported that myosin IX shows processive movement that travels on an actin filament for a long distance. This was an intriguing discovery, because myosin IX is a “single-headed†myosin unlike other processive myosins which have “double-headed†structure. It has been thought that “processive†motors walk on their track with their two heads, thus traveling for a long distance. Therefore, it is reasonable to expect that the processive movement of single headed myosin IX is based on the unique feature of myosin IX motor function. In this study, I investigated the mechanism of processive movement of single-headed myosins by analyzing the mechanism of ATPase cycle of myosin IX that is closely correlated with the cross-bridge cycle (the mechanical cycle of actomyosin). In the first part, I performed the transient enzyme kinetic analysis of myosin IX using the motor domain construct to avoid the complexity raised by the presence of the tail domain. It was revealed that the kinetical characteristics of myosin IX ATPase is quite different from other processive myosins. It was particularly notable that the affinity of the weak actin binding state of Myosin IX was extremely high comparing with known myosins. It is thought that the high affinity for actin throughout the ATPase cycle is a major component to explain the processive movement of myosin IX. In the second part of this study, I cloned full length human myosin IX construct to further investigate the regulation of motor activity of myosin IX. It was revealed that the basal ATPase activity but not the actin dependent ATPase activity of myosin IX is inhibited by its tail region. Furthermore full-length myosin IX is regulated by calcium, presumably due to the calcium binding to the CaM light chain. These result suggest that the tail domain serves as a regulatory component of myosin IX

Community Changes and Social Capital : Organizing Issues based on Previous Studies

MEXT-Supported Program for the Strategic Research Foundation at Private Universities (2014-2018)Forming a Social Well-being Research Consortium in Asi