A first measurement of the interaction cross section of the tau neutrino

The DONuT experiment collected data in 1997 and published first results in 2000 based on four observed $\nu_\tau$ charged-current (CC) interactions. The final analysis of the data collected in the experiment is presented in this paper, based on $3.6 \times 10^{17}$ protons on target using the 800 GeV Tevatron beam at Fermilab. The number of observed $\nu_\tau$ CC interactions is 9, from a total of 578 observed neutrino interactions. We calculated the energy-independent part of the tau-neutrino CC cross section ($\nu + \bar \nu$), relative to the well-known $\nu_e$ and $\nu_\mu$ cross sections. The ratio $\sigma(\nu_\tau)$/$\sigma(\nu_{e,\mu})$ was found to be $1.37\pm0.35\pm0.77$. The $\nu_\tau$ CC cross section was found to be $0.72 \pm 0.24\pm0.36 \times 10^{-38}$ cm$^{2}\rm{GeV}^{-1}$. Both results are in agreement the Standard Model.Comment: 37 pages, 15 figure

圧電材料を用いた損傷自己検知型デバイスの開発とそのシステム化に関する研究

Detecting the damage to the foundations embedded in soil layers is rather difficult when compared with the detection of the damage to the superstructures. Therefore, this study develops a damage-detector device utilizing the piezoelectric materials for the detection. The performance of this device is verified by conducting RC-beam bending tests. The results of the tests exhibit a good correlation between the response of the device, which is compatible to the voltage due to the electric polarization, and the response ductility of the damaged RC-beam specimen.textapplication/pdfdepartmental bulletin pape

Study of Time-Dependent CP Violation in B0→J/ψπ0 Decays

journal articl

Abstracts of Vol.60 Nos1, February 2009

departmental bulletin pape

Structural Basis of the Lactate-dependent Allosteric Regulation of Oxygen Binding in Arthropod Hemocyanin

Hemocyanin (Hc) is an oxygen carrier protein in which oxygen binding is regulated by allosteric effectors such as H+ and l-lactate. Isothermal titration calorimetric measurements showed that l-lactate binds to dodecameric and heterohexameric Hc and to the CaeSS3 homohexamer but not to the CaeSS2 monomer. The binding of lactate caused no change in the optical absorption and x-ray absorption spectra of either oxy- or deoxy-Hc, suggesting that no structural rearrangement of the active site occurred. At pH 6.5, the oxygen binding rate constant kobs obtained by flash photolysis showed a significant increase upon addition of l-lactate, whereas l-lactate addition had little effect at pH 8.3. Lactate binding caused a concentration-dependent shift in the interhexameric distances at pH 6.5 based on small angle x-ray scattering measurements. These results show that l-lactate affects oxygen affinity at pH 6.5 by modulating the global structure of Hc without affecting its binuclear copper center (the active site). In contrast to this, the active site structure of deoxy-Hc is affected by changes in pH (Hirota, S., Kawahara, T., Beltramini, M., Di Muro, P., Magliozzo, R. S., Peisach, J., Powers, L. S., Tanaka, N., Nagao, S., and Bubacco, L. (2008) J. Biol. Chem. 283, 31941-31948). Upon addiction of lactate, the kinetic behavior of oxygen rebinding for Hc was heterogeneous under low oxygen concentrations at pH 6.5 due to changes in the T and R state populations, and the equilibrium was found to shift from the T toward the R state with addition of lactate.journal articl