Difference in the hydration water mobility around F-actin and myosin subfragment-1 studied by quasielastic neutron scattering

Matsuo, Tatsuhito; Arata, Toshiaki*; Oda, Toshiro*; Nakajima, Kenji; Kawamura, Seiko; Kikuchi, Tatsuya; Fujiwara, Satoru

Biochemistry and Biophysics Reports (Internet), 6, p.220 - 225, 2016/07

https://doi.org/10.1016/j.bbrep.2016.04.013

Report of "The 2014 International Forum on Peaceful Use of Nuclear Energy, Nuclear Non-proliferation and Nuclear Security; Future direction toward promoting non-proliferation and the ideal method of developing human resources using Centers of Excellence(COEs) following the New Strategic Energy Plan"

Yamaga, Chikanobu; Tomikawa, Hirofumi; Kobayashi, Naoki; Naoi, Yosuke; Oda, Tetsuzo; Mochiji, Toshiro

JAEA-Review 2015-023, 108 Pages, 2015/10

JAEA-Review-2015-023.pdf:15.22MB

The JAEA held "International Forum on Peaceful Use of Nuclear Energy, Nuclear Non-proliferation and Nuclear Security -Future direction toward promoting non-proliferation and the ideal method of developing human resources using COEs following the New Strategic Energy Plan -" on 3 December 2014. In the Forum, officials and experts from Japan, the United States explained their efforts. Discussion was made in two panels, entitled "Effective and efficient measures to ensure nuclear non-proliferation based on domestic and foreign issues and the direction and role of technology development" and "Roles of nuclear security COEs and future expectations". In Panel Discussion 1, how to implement effective and efficient safeguards was discussed. In Panel Discussion 2, panelists discussed current status of NSSCs and COEs, new role for COEs and regional cooperation. This report includes abstracts of keynote speeches, summaries of two panel discussions and materials of the presentations in the forum.

Difference in hydration structures between F-actin and myosin subfragment-1 detected by small-angle X-ray and neutron scattering

Matsuo, Tatsuhito; Arata, Toshiaki*; Oda, Toshiro*; Fujiwara, Satoru

Biophysics, 9, p.99 - 106, 2013/07

https://doi.org/10.2142/biophysics.9.99

Electrical conduction properties of SiC modified by femtosecond laser

Ito, Takuto*; Deki, Manato; Tomita, Takuro*; Matsuo, Shigeki*; Hashimoto, Shuichi*; Kitada, Takahiro*; Isu, Toshiro*; Onoda, Shinobu; Oshima, Takeshi

Proceedings of 12th International Symposium on Laser Precision Microfabrication (LPM 2011) (Internet), 5 Pages, 2011/06

Enhancement of local electrical conductivities in SiC by femtosecond laser modification

Deki, Manato; Ito, Takuto*; Yamamoto, Minoru*; Tomita, Takuro*; Matsuo, Shigeki*; Hashimoto, Shuichi*; Kitada, Takahiro*; Isu, Toshiro*; Onoda, Shinobu; Oshima, Takeshi

Applied Physics Letters, 98(13), p.133104_1 - 133104_3, 2011/03

https://doi.org/10.1063/1.3573786

Reconstitution of the muscle thin filament from recombinant troponin components and the native thin filaments

Matsumoto, Fumiko; Deshimaru, Shungo*; Oda, Toshiro*; Fujiwara, Satoru

Analytical Biochemistry, 399(2), p.299 - 301, 2010/04

https://doi.org/10.1016/j.ab.2010.01.004

We have developed a technique by which muscle thin filaments are reconstituted from the recombinant troponin components and the native thin filaments. By this technique, the reconstituted troponin complex is exchanged into the native thin filaments in the presence of 20% glycerol and 0.3 M KCl at pH 6.2. Over 90% of endogenous troponin complex was replaced with the recombinant troponin complex. Structural integrity and Ca-sensitivity of the reconstituted thin filament prepared by this technique was confirmed by X-ray fiber diffraction measurements and the thin filament activated myosin subfragment 1 ATPase measurements, respectively.

Differences in internal dynamics of actin under different structural states detected by neutron scattering

Fujiwara, Satoru; Plazanet, M.*; Matsumoto, Fumiko; Oda, Toshiro*

Biophysical Journal, 94(12), p.4880 - 4889, 2008/06

https://doi.org/10.1529/biophysj.107.125302

Actin plays crucial roles in various aspects of cell motility. Flexibility of F-actin, a filamentous polymer formed by polymerization of the monomers (G-actin), is important for such a variety of functions. This flexibility allows F-actin to interact with various proteins, thereby expressing multiple functions. Understanding the variety of functions of actin thus requires understanding the flexibility of F-actin. As a first step towards this ultimate purpose, we carried out elastic incoherent neutron scattering (EINS) experiments on G-actin and F-actin under hydrated states. The mean square displacement (MSD) was estimated from the EINS measurements. Temperature dependence of MSD showed that two dynamical transitions occur at about 150 K and about 245 K, and that behavior of MSD is different between G-actin and F-actin, such that G-actin is "softer" than F-actin. The different behavior observed is ascribed to the differences in dynamical heterogeneity between F-actin and G-actin.

Structural analysis of troponin mutants causing cardiomyopathy by small-angle X-ray scattering

Fujiwara, Satoru; Yonezawa, Yasushige*; Matsumoto, Fumiko; Oda, Toshiro*; Takeda, Soichi*

no journal, , 

no abstracts in English

Polarization dependence of local electric conductivities in femtosecond laser modified SiC

Ito, Takuto*; Deki, Manato; Tomita, Takuro*; Matsuo, Shigeki*; Hashimoto, Shuichi*; Kitada, Takahiro*; Isu, Toshiro*; Onoda, Shinobu; Oshima, Takeshi

no journal, , 

no abstracts in English

Relationship between the water dynamics and the internal dynamics of actin studied by quasi-elastic neutron scattering

Fujiwara, Satoru; Plazanet, M.*; Oda, Toshiro*

no journal, ,