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Journal Articles

How different is the core of $$^{25}$$F from $$^{24}$$O$$_{g.s.}$$ ?

Tang, T. L.*; Uesaka, Tomohiro*; Kawase, Shoichiro; Beaumel, D.*; Dozono, Masanori*; Fujii, Toshihiko*; Fukuda, Naoki*; Fukunaga, Taku*; Galindo-Uribarri, A.*; Hwang, S. H.*; et al.

Physical Review Letters, 124(21), p.212502_1 - 212502_6, 2020/05

 Times Cited Count:14 Percentile:74.77(Physics, Multidisciplinary)

The structure of a neutron-rich $$^{25}$$F nucleus is investigated by a quasifree ($$p,2p$$) knockout reaction. The sum of spectroscopic factors of $$pi 0d_{5/2}$$ orbital is found to be 1.0 $$pm$$ 0.3. The result shows that the $$^{24}$$O core of $$^{25}$$F nucleus significantly differs from a free $$^{24}$$O nucleus, and the core consists of $$sim$$35% $$^{24}$$O$$_{rm g.s.}$$, and $$sim$$65% excited $$^{24}$$O. The result shows that the $$^{24}$$O core of $$^{25}$$F nucleus significantly differs from a free $$^{24}$$O nucleus. The result may infer that the addition of the $$0d_{5/2}$$ proton considerably changes the neutron structure in $$^{25}$$F from that in $$^{24}$$O, which could be a possible mechanism responsible for the oxygen dripline anomaly.

Journal Articles

An Insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle X-ray and neutron scattering study

Yonezawa, Yasushige*; Tanaka, Shimpei*; Kubota, Tomomi*; Wakabayashi, Katsuzo*; Yutani, Katsuhide*; Fujiwara, Satoru

Journal of Molecular Biology, 323(2), p.237 - 251, 2002/10

 Times Cited Count:74 Percentile:74.85(Biochemistry & Molecular Biology)

It is known that hen egg white lysozyme (HEWL) forms amyloid fibrils in highly concentrated ethanol solutions. In order to gain an insight into the mechanism of the amyloid fibril formation, the structures of HEWL in solutions of various protein and ethanol concentrations were investigated with small-angle X-ray and neutron scattering. It was shown that the structural states of HEWL were distinguished as the monomer state, the state of the dimer formation, the state of the protofilament formation, the protofilament state, and the state towards the formation of the amyloid fibrils. Circular dichroism measurements showed that the large changes in the secondary structures of HEWL occurred during the dimer formation. Structural characterization showed that the dimers had an elongated shape, the protofilaments were formed by stacking of the dimers with their long axis (nearly) perpendicular to the protofilament axis, and the changes of the structural states towards the amyloid fibril formation occurred via lateral association of the protofilaments.

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