Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Tominaga, Taiki*; Nakagawa, Hiroshi; Sahara, Masae*; Oda, Takashi*; Inoue, Rintaro*; Sugiyama, Masaaki*
Life (Internet), 12(5), p.675_1 - 675_9, 2022/05
Times Cited Count：0 Percentile：0.01(Biology)The background scattering of sample cells suitable for aqueous protein solution samples, conducted with a neutron backscattering spectrometer, was evaluated. It was found that the scattering intensity of an aluminum sample cell coated with boehmite using D
O was lower than that of a sample cell coated with regular water (HO). In addition, meticulous attention to cells with small individual weight differences and the positional reproducibility of the sample cell relative to the spectrometer neutron beam position enabled the accurate subtraction of the scattering profiles of the DO buffer and the sample container. Consequently, high quality information on protein dynamics could be extracted from dilute protein solutions.
Tominaga, Taiki*; Sahara, Masae*; Kawakita, Yukinobu; Nakagawa, Hiroshi; Yamada, Takeshi*
Journal of Applied Crystallography, 54(6), p.1631 - 1640, 2021/12
Times Cited Count：4 Percentile：55.82(Chemistry, Multidisciplinary)Nogami, Satoshi*; Kadota, Kazunori*; Uchiyama, Hiromasa*; Arima-Osonoi, Hiroshi*; Iwase, Hiroki*; Tominaga, Taiki*; Yamada, Takeshi*; Takata, Shinichi; Shibayama, Mitsuhiro*; Tozuka, Yuichi*
International Journal of Biological Macromolecules, 190, p.989 - 998, 2021/11
Times Cited Count：6 Percentile：39.73(Biochemistry & Molecular Biology)Nakagawa, Hiroshi; Saio, Tomohide*; Nagao, Michihiro*; Inoue, Rintaro*; Sugiyama, Masaaki*; Ajito, Satoshi; Tominaga, Taiki*; Kawakita, Yukinobu
Biophysical Journal, 120(16), p.3341 - 3354, 2021/08
Times Cited Count：4 Percentile：38.66(Biophysics)A multi-domain protein can have various conformations in solution. Interactions with other molecules result in the stabilization of one of the conformations and change in the domain dynamics. SAXS, a well-established experimental technique, can be employed to elucidate the conformation of a multi-domain protein in solution. NSE spectroscopy is a promising technique for recording the domain dynamics in nanosecond and nanometer scale. Despite the great efforts, there are still under development. Thus, we quantitatively removed the contribution of diffusion dynamics and hydrodynamic interactions from the NSE data via incoherent scattering, revealing the differences in the domain dynamics of the three functional states of a multi-domain protein, MurD. The differences among the three states can be explained by two domain modes.
Tominaga, Taiki*; Sahara, Masae*; Kawakita, Yukinobu; Nakagawa, Hiroshi; Shimamoto, Naonobu*
JPS Conference Proceedings (Internet), 33, p.011094_1 - 011094_5, 2021/03
In quasielastic neutron scattering studies, aluminum or aluminum alloys are frequently employed as sample cells. With the increasing incident-neutron flux, the research area currently continues to expand; thus, obtaining data has become quicker than ever for dilute conditions. One such area is the water-containing systems. In this study, we investigated the effect of temperature on Al and found that even in a low temperature atmosphere, Al corrosion can occur. This was attributed to the different thermal expansion coefficients of Al as a base substrate and Al oxide as a passivating film.
Matsuura, Masato*; Yamada, Takeshi*; Tominaga, Taiki*; Kobayashi, Makoto*; Nakagawa, Hiroshi; Kawakita, Yukinobu
JPS Conference Proceedings (Internet), 33, p.011068_1 - 011068_6, 2021/03
The position dependence of the scattered intensity in the time-of-flight backscattering spectrometer DNA was investigated. A periodic structure for both vertical (pixel) and horizontal (PSD) directions was observed. The solar slit and over-bending of an analyzer crystal is discussed as a possible origin of the modulation in the intensity. We have developed software program for the systematic correction of the position-dependent intensity and offset energy for the elastic peak. This corrects the deviation from the true scattering intensity and improve the quality of the data, which includes the energy resolution.
Tominaga, Taiki*; Kawakita, Yukinobu; Nakagawa, Hiroshi; Yamada, Takeshi*; Shibata, Kaoru
JPS Conference Proceedings (Internet), 33, p.011086_1 - 011086_5, 2021/03
We developed a quartz double cylindrical sample cell optimized for a backscattering neutron spectrometer, especially for BL02 (DNA), MLF in J-PARC. A quartz glass tube, with one end closed, is shaved to obtain a wall thickness of 0.55 mm. The inner tube is properly centered using a protrusion into the outer tube such that the interstice between the outer and inner tubes keeps constant. This quartz cell can be used for samples that should not be in contact with the aluminum surface. We verified cell's background effect between the quartz cell and Al cell by QENS measurements using DO buffer. The elastic intensity profiles of the buffer in a low Q region were identical between both quartz cell and Al cell (A1070). In a high Q region, however, the profiles were different caused by the first sharp diffraction peak of quartz glass. For this region the data should be analyzed by consideration of absorption correction and diffraction in individual thickness of quartz cell.
Inoue, Rintaro*; Oda, Takashi*; Nakagawa, Hiroshi; Tominaga, Taiki*; Saio, Tomohide*; Kawakita, Yukinobu; Shimizu, Masahiro*; Okuda, Aya*; Morishima, Ken*; Sato, Nobuhiro*; et al.
Scientific Reports (Internet), 10, p.21678_1 - 21678_10, 2020/12
Times Cited Count：3 Percentile：13.48(Multidisciplinary Sciences)Incoherent quasielastic neutron scattering (iQENS) is a fascinating technique for investigating the internal dynamics of protein. However, both low flux of neutron beam and absence of analytical procedure for extracting the internal dynamics from iQENS profile have been obstacles for studying it under physiological condition (in solution). Thanks to the recent development of neutron source, spectrometer and computational technique, they enable us to decouple internal dynamics, translational and rotational diffusions from the iQENS profile. The internal dynamics of two proteins: globular domain protein (GDP) and intrinsically disordered protein (IDP) in solution were studied. It was found that the average relaxation rate of IDP was larger than that of GDP. Through the detailed analyses on their internal dynamics, it was revealed that the fraction of mobile H atoms in IDP was much higher than that in GDP. Interestingly, the fraction of mobile H atoms was closely related to the fraction of H atoms on highly solvent exposed surfaces. The iQENS study presented that the internal dynamics were governed by the highly solvent exposed amino acid residues depending upon protein molecular architectures.
Makuuchi, Keizo; Tagawa, Seiichi*; Kashiwagi, Masayuki*; Kamada, Toshimitsu*; Sekiguchi, Masayuki*; Hosobuchi, Kazunari*; Tominaga, Hiroshi*; Ooka, Norikazu
Journal of Nuclear Science and Technology, 39(9), p.1002 - 1007, 2002/09
Times Cited Count：6 Percentile：39.54(Nuclear Science & Technology)no abstracts in English
Takehisa, Masaaki*; Tagawa, Seiichi*; Kashiwagi, Masayuki*; Tominaga, Hiroshi*; Ishikawa, Isamu*; Ooka, Norikazu; Kamada, Toshimitsu*; Hosobuchi, Kazunari*; Makuuchi, Keizo; Takeshita, Hidefumi; et al.
Genshiryoku Riyo No Keizai Kibo; NSA/Commentaries, No.9, 139 Pages, 2001/01
no abstracts in English
Abe, Fumitoshi*; Ota, Shizuko*; Kosako, Toshiso*; Tanaka, Ryuichi; Tominaga, Hiroshi*; Yamamoto, Masago*; Ujihira, Yusuke*
Isotope News, (501), p.16 - 26, 1996/02
no abstracts in English
Tominaga, Hiroshi; Ishikawa, Isamu
Nucl. Geophys., 5(1-2), p.137 - 140, 1991/00
no abstracts in English
Tominaga, Hiroshi
Nihon Genshiryoku Gakkai-Shi, 32(7), p.670 - 673, 1990/07
no abstracts in English
Tominaga, Hiroshi
Isotope News, 8, p.24 - 27, 1989/08
no abstracts in English
*; *; *; Tominaga, Hiroshi; ; Tachikawa, Noboru
Nucl. Geophys., 3(2), p.147 - 156, 1989/00
no abstracts in English
Tominaga, Hiroshi
Shimpan Genshiryoku Handobukku, p.669 - 685, 1989/00
no abstracts in English
Ishikawa, Isamu; Tachikawa, Noboru; Okubo, Makio; Tominaga, Hiroshi
Transactions of the American Nuclear Society, 56(SUPPL.3), p.31 - 32, 1988/00
no abstracts in English
*; *; *; *; Tominaga, Hiroshi; ; Tachikawa, Noboru
Transactions of the American Nuclear Society, SUPPL.56(3), p.21 - 22, 1988/00
no abstracts in English
Tominaga, Hiroshi
Radioisotopes, 36(8), p.428 - 431, 1987/08
no abstracts in English
*; *; *; *; Tominaga, Hiroshi; ; *
Proc. 1987 Int. Waste Management Conf., p.303 - 308, 1987/00
no abstracts in English
