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Journal Articles

Cross-scale analysis of temperature compensation in the cyanobacterial circadian clock system

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

Journal Articles

Segmental motions of proteins under non-native states evaluated using quasielastic neutron scattering

Fujiwara, Satoru*; Matsuo, Tatsuhito*; Sugimoto, Yasunobu*; Shibata, Kaoru

Journal of Physical Chemistry Letters (Internet), 10(23), p.7505 - 7509, 2019/12

 Times Cited Count:0 Percentile:0.01(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.

Journal Articles

Dynamic properties of human $$alpha$$-synuclein related to propensity to amyloid fibril formation

Fujiwara, 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:3 Percentile:27.91(Biochemistry & Molecular Biology)

$$alpha$$-synuclein ($$alpha$$Syn) is an intrinsically disordered protein (IDP) with unknown function. $$alpha$$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 $$alpha$$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 $$alpha$$Syn. These results imply that fibril formation of $$alpha$$Syn requires not only the enhanced local motions but also the segmental motions such that the proper inter-molecular interactions are possible.

Journal Articles

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

Journal Articles

Dynamical behavior of human $$alpha$$-synuclein studied by quasielastic neutron scattering

Fujiwara, 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:18 Percentile:67.4(Multidisciplinary Sciences)

Journal Articles

Spin hydrodynamic generation

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:65 Percentile:95.17(Physics, Multidisciplinary)

Journal Articles

Structures of the troponin core domain containing the cardiomyopathy-causing mutants studied by small-angle X-ray scattering

Matsuo, Tatsuhito; Takeda, Soichi*; Oda, Toshiro*; Fujiwara, Satoru

Biophysics and Physicobiology (Internet), 12, p.145 - 158, 2015/12

Journal Articles

Barnett effect in paramagnetic states

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:19 Percentile:68.15(Materials Science, Multidisciplinary)

Journal Articles

Line splitting by mechanical rotation in nuclear magnetic resonance

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:10 Percentile:48.8(Physics, Applied)

Journal Articles

Internal dynamics of 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

Biochemical and Biophysical Research Communications, 459(3), p.493 - 497, 2015/04

 Times Cited Count:4 Percentile:16.86(Biochemistry & Molecular Biology)

Journal Articles

Observation of Barnett fields in solids by nuclear magnetic resonance

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:35 Percentile:84.13(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.

Journal Articles

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

Journal Articles

Dynamics of cardiomyopathy-causing mutant of troponin measured by neutron scattering

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:1 Percentile:12.72(Physics, Multidisciplinary)

Troponin is a protein that regulates the muscle contraction depending on the intracellular Ca$$^{2+}$$ 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$$^{2+}$$ signal transmission mechanism, leading to the functional aberration.

Journal Articles

Isoscalar giant resonances in the Sn nuclei and implications for the asymmetry term in the nuclear-matter incompressibility

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:92 Percentile:97.51(Physics, Nuclear)

JAEA Reports

The Technological study on the decommissioning of nuclear facility, etc. in the Tokai Research Establishment

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

Journal Articles

Dynamic properties of lithium ions in lithium ceramics

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

Oral presentation

Structural changes of troponin by cardiomyopathy-causing mutations

Fujiwara, Satoru; Matsuo, Tatsuhito; Matsumoto, Fumiko; Oda, Toshiro*; Takeda, Soichi*

no journal, , 

Oral presentation

Study on event progression in PLOHS for JSFR, 1; Numerical simulation of plant dynamics phase in PLOHS

Matsuo, Eiji*; Watanabe, Motoko*; Yamada, Yumi*; Koyama, Kazuya*; Shimakawa, Yoshio*; Sato, Mitsuru*; Kamishima, Yoshio*; Yokoi, Shinobu*; Yamano, Hidemasa; Suzuki, Toru; et al.

no journal, , 

Event transition in PLOHS is investigated to contribute to Level 2 PSA focused on JSFR. This report will describes about the evaluation result of the event escalation in the response transition after PLOHS.

Oral presentation

Dynamics of cardiomyopathy-causing mutant of troponin observed by neutron scattering

Matsuo, Tatsuhito; Natali, F.*; Zaccai, G.*; Fujiwara, Satoru

no journal, , 

Troponin is a protein that regulates the muscle contraction depending on the intracellular Ca2+ 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 Ca2+ signal transmission mechanism, leading to the functional aberration.

Oral presentation

Internal dynamics of protein during amyloid fibril formation observed by neutron scattering

Fujiwara, Satoru; Yamada, Takeshi*; Matsuo, Tatsuhito; Takahashi, Nobuaki; Kamazawa, Kazuya*; Kawakita, Yukinobu; Shibata, Kaoru*

no journal, , 

52 (Records 1-20 displayed on this page)