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Tada, Junichiro*; Nakashima, Hiroshi; Hayano, Ryugo*; Kobayashi, Hitoshi*; Asano, Yoshihiro*
Wakariyasui Hoshasen Butsurigaku; Kaitei 3-Han, 305 Pages, 2018/03
This book is an introduction to radiation physics. Under the concept of "linking physics of high school and radiation physics" for readers with high school graduation degree, we are doing simple commentary on the basis of qualitative explanation as much as possible. This book begins with "What is Radiation Physics", and consists of 12 chapters, including introductory special relativity, introductory quantum theory, structures of atoms and nuclei, radiations, radioactivity, interactions between radiation and matter, accelerators, radiation dose and so on.
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ceramics fabricated by high-pressure sinteringKitada, Kazuya*; Kobune, Masafumi*; Adachi, Wataru*; Yazawa, Tetsuo*; Saito, Hiroyuki; Aoki, Katsutoshi; Mizuki, Junichiro; Ishikawa, Kenya*; Hiranaga, Yoshiomi*; Cho, Yasuo*
Chemistry Letters, 37(5), p.560 - 561, 2008/05
Times Cited Count：9 Percentile：37.55(Chemistry, Multidisciplinary)Yamada, Hidenori*; Tamada, Taro; Kosaka, Megumi*; Miyata, Kohei*; Fujiki, Shinya*; Tano, Masaru*; Moriya, Masayuki*; Yamanishi, Mamoru*; Honjo, Eijiro; Tada, Horiko*; et al.
Protein Science, 16(7), p.1389 - 1397, 2007/07
Times Cited Count：39 Percentile：59.5(Biochemistry & Molecular Biology)In an attempt to control protein incorporation in a crystal lattice, a leucine zipper-like hydrophobic interface (comprising four leucine residues) was introduced into a helical region (helix 2) of the human pancreatic ribonuclease 1 (RNase 1) that was predicted to form a suitable crystallization interface. Although crystallization of wild type RNase 1 has not yet been reported, the RNase 1 mutant having four leucines (4L-RNase 1) was successfully crystallized under several different conditions. The crystal structures were subsequently determined by X-ray crystallography by molecular replacement using the structure of bovine RNase A. The overall structure of 4L-RNase 1 is quite similar to that of the bovine RNase A, and the introduced leucine residues formed the designed crystal interface. To further characterize the role of the introduced leucine residues in crystallization of RNase 1, the number of leucines was reduced to three or two (3L- and 2L-RNase 1, respectively). Both mutants crystallized and a similar hydrophobic interface as in 4L-RNase 1 was observed. A related approach to engineer crystal contacts at helix 3 of RNase 1 (N4L-RNase 1) was also evaluated. N4L-RNase 1 also successfully crystallized, and formed the expected hydrophobic packing interface. These results suggest that appropriate introduction of a leucine zipper-like hydrophobic interface can promote intra molecular symmetry for more efficient protein crystallization in crystal lattice engineering efforts.
Kobune, Masafumi*; Fukushima, Koji*; Yamaji, Toru*; Tada, Hideto*; Yazawa, Tetsuo*; Fujisawa, Hironori*; Shimizu, Masaru*; Nishihata, Yasuo; Matsumura, Daiju; Mizuki, Junichiro; et al.
Journal of Applied Physics, 101(7), p.074110_1 - 074110_6, 2007/04
Times Cited Count：8 Percentile：33.21(Physics, Applied)no abstracts in English
