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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
Niimura, Nobuo; Chatake, Toshiyuki; Ostermann, A.; Kurihara, Kazuo; Tanaka, Ichiro
Zeitschrift f
r Kristallographie, 218(2), p.96 - 107, 2003/03
no abstracts in English
-radiationYokoya, Akinari; Cunniffe, S. M. T.*; O'Neill, P.*
Journal of the American Chemical Society, 124(30), p.8859 - 8866, 2002/07
Times Cited Count：87 Percentile：87.69(Chemistry, Multidisciplinary)no abstracts in English
Takahashi, Yoshio*; Tada, Akisa*; Kimura, Takaumi; Shimizu, Hiroshi*
Chemistry Letters, (6), p.700 - 701, 2000/06
no abstracts in English
Niimura, Nobuo*; Minezaki, Yoshiaki
Nihon Kessho Gakkai-Shi, 40(1), p.114 - 118, 1998/00
no abstracts in English
Niimura, Nobuo; Minezaki, Yoshiaki; *; J.C.Castagna*; F.Cipriani*; P.Hoghoj*; M.S.Lehmann*; C.Wilkinson*
Nature Structural Biology, 4(11), p.909 - 914, 1997/11
Times Cited Count：143 Percentile：94.91(Biochemistry & Molecular Biology)no abstracts in English
Niimura, Nobuo*
Tampakushitsu Kakusan Koso, 39(7), p.1283 - 1288, 1994/00
no abstracts in English
Matsuo, Tatsuhito; Arata, Toshiaki*; Oda, Toshiro*; Fujiwara, Satoru
no journal, ,
In this study, we investigated the dynamics of the hydration water around F-actin and myosin S1, which are proteins interacting with each other to produce force in muscle contraction, by quasielastic neutron scattering (QENS). The QENS measurements were conducted on the solution samples of F-actin (150 mg/ml) and S1 (80 mg/ml) in H
O and DO using the cold-neutron disk-chopper spectrometer AMATERAS in MLF/J-PARC, Japan. The spectra of hydration water were obtained by subtracting those of proteins and those of bulk water from the measured spectra of HO samples (the spectra of proteins were obtained by subtracting those of DO buffer from those of DO samples, while the spectra of HO buffer was used as those of bulk water) with appropriate scaling factors. The translational diffusion coefficients(D
) and the residence time (
) were evaluated from the dependence of the half-widths at half-maximum of the Lorentzian functions fit to the spectra on the momentum transfer. In the current analysis, it was found that the D value of the hydration water around S1was smaller than that of bulk water while the value was larger than that of bulk water, suggesting that S1 has typical hydration water, the mobility of which is less than that of bulkwater. On the other hand, both the D and the values of the hydration water around F-actin were closer to those of bulk water, suggesting that the hydration water around F-actin has higher mobility than that around other proteins including S1. The results of a more detailed analysis will be given in the presentation.
Matsuo, Tatsuhito; Arata, Toshiaki*; Oda, Toshiro*; Fujiwara, Satoru
no journal, ,
The dynamics of F-actin and myosin S1, and their hydration water were studied by quasielastic neutron scattering (QENS). Analysis of the spectra found that a larger fraction of the atoms of F-actin undergoes the motions with the smaller residence time than S1. It was also found that the mobility of the hydration water of S1 is lower than that of bulk water, while that of the hydration water of F-actin is slightly higher than that of bulk water, evaluated by their translational diffusion coefficient and the residence time. These results suggest that the concerted action of rapidly fluctuating F-actin and its hydration water allows F-actin to explore a wide range of the conformational space, which would facilitate the binding of myosin to F-actin.
Matsuo, Tatsuhito; Arata, Toshiaki*; Oda, Toshiro*; Fujiwara, Satoru
no journal, ,
The picosecond dynamics of F-actin, myosin S1, and their hydration water were studied by quasielastic neutron scattering (QENS) at J-PARC. Analysis of the QENS spectra showed that a larger fraction of the atoms of F-actin undergoes the motions with the smaller residence time than S1. It was also found that the mobility of the hydration water of S1, which was evaluated from the translational diffusion coefficient, the residence time, and the rotational correlation time, is lower than that of bulk water, while that of the hydration water of F-actin is close to that of bulk water. These results suggest that the concerted action of rapidly fluctuating F-actin and its hydration water allows F-actin to explore a wide range of the conformational space, which would facilitate the binding of myosin to F-actin.
Yonetani, Yoshiteru
no journal, ,
