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Furuike, Yoshihiko*; Ouyang, D.*; Tominaga, Taiki*; Matsuo, Tatsuhito*; Mukaiyama, Atsushi*; Kawakita, Yukinobu; Fujiwara, Satoru*; Akiyama, Shuji*
Communications Physics (Internet), 5(1), p.75_1 - 75_12, 2022/04
Times Cited Count：6 Percentile：61.96(Physics, Multidisciplinary)
O
submicron particles studied by polarized small-angle neutron scatteringNomura, Eiji*; Chiba, Momoko*; Matsuo, Sakoto*; Noda, Chiaki*; Kobayashi, Satoru*; Manjanna, J.*; Kawamura, Yukihiko*; Oishi, Kazuki*; Hiroi, Kosuke; Suzuki, Junichi*
AIP Advances (Internet), 12(3), p.035034_1 - 035034_5, 2022/03
Times Cited Count：5 Percentile：44.76(Nanoscience & Nanotechnology)Fujiwara, Satoru*; Matsuo, Tatsuhito*; Sugimoto, Yasunobu*; Shibata, Kaoru
Journal of Physical Chemistry Letters (Internet), 10(23), p.7505 - 7509, 2019/12
Times Cited Count：4 Percentile：18.13(Chemistry, Physical)Characterization of the dynamics of disordered polypeptide chains is required to elucidate the behavior of intrinsically disordered proteins and proteins under non-native states related to the folding process. Here we develop a method using quasielastic neutron scattering, combined with small-angle X-ray scattering and dynamic light scattering, to evaluate segmental motions of proteins as well as diffusion of the entire molecules and local side-chain motions. We apply this method to RNase A under the unfolded and molten-globule (MG) states. The diffusion coefficients arising from the segmental motions are evaluated and found to be different between the unfolded and MG states. The values obtained here are consistent with those obtained using the fluorescence-based techniques. These results demonstrate not only feasibility of this method but also usefulness to characterize the behavior of proteins under various disordered states.
-synuclein related to propensity to amyloid fibril formationFujiwara, Satoru*; Kono, Fumiaki*; Matsuo, Tatsuhito*; Sugimoto, Yasunobu*; Matsumoto, Tomoharu*; Narita, Tetsuhiro*; Shibata, Kaoru
Journal of Molecular Biology, 431(17), p.3229 - 3245, 2019/08
Times Cited Count：15 Percentile：50.84(Biochemistry & Molecular Biology)-synuclein (Syn) is an intrinsically disordered protein (IDP) with unknown function. Syn is known to form amyloid fibrils, which are implicated with the pathogenesis of Parkinson's disease and other synucleinopathies. Elucidating the mechanism of fibril formation of Syn is therefore important for understanding the mechanism of the pathogenesis of these diseases. Here, using the quasielastic neutron scattering (QENS) and small-angle X-ray scattering (SAXS) techniques, we investigated the dynamic and structural properties of Syn. These results imply that fibril formation of Syn requires not only the enhanced local motions but also the segmental motions such that the proper inter-molecular interactions are possible.
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
-synuclein studied by quasielastic neutron scatteringFujiwara, Satoru; Araki, Katsuya*; Matsuo, Tatsuhito; Yagi, Hisashi*; Yamada, Takeshi*; Shibata, Kaoru; Mochizuki, Hideki*
PLOS ONE (Internet), 11(4), p.e0151447_1 - e0151447_17, 2016/04
Times Cited Count：26 Percentile：64.21(Multidisciplinary Sciences)Takahashi, Ryo*; Matsuo, Mamoru; Ono, Masao; Harii, Kazuya; Chudo, Hiroyuki; Okayasu, Satoru; Ieda, Junichi; Takahashi, Saburo*; Maekawa, Sadamichi; Saito, Eiji
Nature Physics, 12, p.52 - 56, 2016/01
Times Cited Count：117 Percentile：96.13(Physics, Multidisciplinary)Matsuo, Tatsuhito; Takeda, Soichi*; Oda, Toshiro*; Fujiwara, Satoru
Biophysics and Physicobiology (Internet), 12, p.145 - 158, 2015/12
Ono, Masao; Chudo, Hiroyuki; Harii, Kazuya; Okayasu, Satoru; Matsuo, Mamoru; Ieda, Junichi; Takahashi, Ryo*; Maekawa, Sadamichi; Saito, Eiji
Physical Review B, 92(17), p.174424_1 - 174424_4, 2015/11
Times Cited Count：34 Percentile：75.81(Materials Science, Multidisciplinary)Harii, Kazuya; Chudo, Hiroyuki; Ono, Masao; Matsuo, Mamoru; Ieda, Junichi; Okayasu, Satoru; Maekawa, Sadamichi; Saito, Eiji
Japanese Journal of Applied Physics, 54(5), p.050302_1 - 050302_3, 2015/05
Times Cited Count：13 Percentile：47.44(Physics, Applied)Matsuo, Tatsuhito; Arata, Toshiaki*; Oda, Toshiro*; Nakajima, Kenji; Kawamura, Seiko; Kikuchi, Tatsuya; Fujiwara, Satoru
Biochemical and Biophysical Research Communications, 459(3), p.493 - 497, 2015/04
Times Cited Count：5 Percentile：15.33(Biochemistry & Molecular Biology)Chudo, Hiroyuki; Ono, Masao; Harii, Kazuya; Matsuo, Mamoru; Ieda, Junichi; Haruki, Rie*; Okayasu, Satoru; Maekawa, Sadamichi; Yasuoka, Hiroshi; Saito, Eiji
Applied Physics Express, 7(6), p.063004_1 - 063004_4, 2014/06
Times Cited Count：49 Percentile：85.05(Physics, Applied)A magnetic field is predicted to emerge on a particle in a rotating body even if the body is electrically neutral. This emergent field is called a Barnett field. We show that nuclear magnetic resonance (NMR) enables direct measurement of the Barnett field in solids. We rotated both a sample and an NMR coil synchronously at high speed and found an NMR shift whose sing reflects that of the nuclear magnetic moments. This result provides direct evidence of the Barnett field. The use of NMR for Barnett field measurement enables the unknown signs of nuclear magnetic moments in solids to be determined.
Matsuo, Tatsuhito; Arata, Toshiaki*; Oda, Toshiro*; Fujiwara, Satoru
Biophysics, 9, p.99 - 106, 2013/07
Matsuo, Tatsuhito; Natali, F.*; Plazanet, M.*; Zaccai, G.*; Fujiwara, Satoru
Journal of the Physical Society of Japan, 82(Suppl.A), p.SA020_1 - SA020_5, 2013/01
Times Cited Count：3 Percentile：26.44(Physics, Multidisciplinary)Troponin is a protein that regulates the muscle contraction depending on the intracellular Ca
concentration. K247R mutation of TnT is known to cause the hypertrophic cardiomyopathy. In this work, neutron scattering was used to detect possible changes in dynamics of troponin caused by mutation. Elastic incoherent neutron scattering experiments were carried out on solution samples of the wild type, and K247R mutant at the IN13 spectrometer at the Institut Laue-Langevin, at temperatures between 280 K and 292 K with an interval of 3 K. From the measured scattering data, force constants (
k
), which reflect the resilience of the protein, were calculated. The k values for the wild type and K247R mutant were 0.077 (0.035) N/m and 0.046 (0.026) N/m (mean(s.d.)), respectively. This suggests that the disease-causing mutant is more flexible than the wild type. The large flexibility might modulate Ca signal transmission mechanism, leading to the functional aberration.
Li, T.*; Garg, U.*; Liu, Y.*; Marks, R.*; Nayak, B. K.*; Madhusudhana Rao, P. V.*; Fujiwara, Mamoru*; Hashimoto, Hisanobu*; Nakanishi, Kosuke*; Okumura, Shun*; et al.
Physical Review C, 81(3), p.034309_1 - 034309_11, 2010/03
Times Cited Count：115 Percentile：97.60(Physics, Nuclear)Tomii, Hiroyuki; Matsuo, Kiyoshi*; Shiraishi, Kunio; Kato, Rokuro; Watabe, Kozo; Higashiyama, Yutaka; Nagane, Satoru*; Hanawa, Yukimitsu*
JAERI-Tech 2005-017, 65 Pages, 2005/03
JAERI-Tech-2005-017.pdf:3.79MB
no abstracts in English
Igawa, Naoki; Ono, Hideo; Nagasaki, Takanori; Ishii, Yoshinobu; Noda, Kenji; Watanabe, H.; Matsuo, Toru*; Igarashi, Kazuo*
Ceramic Transactions, Vol.27, p.135 - 156, 1992/00
no abstracts in English
Fujiwara, Satoru; Yamada, Takeshi*; Matsuo, Tatsuhito; Takahashi, Nobuaki; Kamazawa, Kazuya*; Kawakita, Yukinobu; Shibata, Kaoru*
no journal, ,
no abstracts in English
Fujiwara, Satoru; Yamada, Takeshi*; Matsuo, Tatsuhito; Takahashi, Nobuaki; Kamazawa, Kazuya*; Kawakita, Yukinobu; Shibata, Kaoru*
no journal, ,
no abstracts in English
Fujiwara, Satoru; Yamada, Takeshi*; Matsuo, Tatsuhito; Takahashi, Nobuaki; Kamazawa, Kazuya*; Kawakita, Yukinobu; Shibata, Kaoru*
no journal, ,
