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藤原 悟; 荒木 克哉*; 松尾 龍人; 八木 寿梓*; 山田 武*; 柴田 薫; 望月 秀樹*
PLOS ONE (Internet), 11(4), p.e0151447_1 - e0151447_17, 2016/04
被引用回数:24 パーセンタイル:65.34(Multidisciplinary Sciences)Filamentous aggregates (amyloid fibrils) of the protein -synuclein (-Syn) are related to the pathogenesis of Parkinson's disease. To understand the pathogenesis mechanism of this disease, the mechanism of the amyloid fibril formation of -Syn must be elucidated. As a first step toward this ultimate goal, dynamical behavior of -Syn in the monomeric and the fibril states was investigated using quasielastic neutron scattering (QENS). Analysis of the QENS spectra of solution samples of -Syn shows that diffusive global motions are observed in the monomeric state but largely suppressed in the fibril state. However, the amplitude of the side chain motion is shown to be larger in the fibril state than in the monomeric state. This implies that significant solvent space exists within the fibrils, which is attributed to the -Syn molecules within the fibrils having a distribution of conformations. The larger amplitude of the side chain motion in the fibril state than in the monomeric state implies that the fibril state is entropically favorable.
神村 誠二*; 柳生 秀樹*; 望月 修*; 大西 隆雄*; 八木 敏明; 瀬口 忠男
DEI-91-131, p.11 - 19, 1991/12
原子力発電所の主要な機器の一つである電線・ケーブルの寿命を精度高く予測する方法を開発するために、妥当な促進劣化試験方法およびケーブルの非破壊診断方法の研究を行った。2種類の低圧用CVケーブル(架橋PE絶縁/PVCシース)について、使用環境の基準条件(1Gy/h,50C)での劣化速度の20倍~300倍の加速劣化を行い、機械特性の変化を調べた。また、ケーブルの劣化は開発した劣化診断装置を用い、トルク値の測定より検討した。2種類のCVケーブルについて、加速試験による加速倍率の依存性から寿命を算出できる見通しが得られた。開発した小型の劣化診断装置を用いて求めたケーブルのトルク値とシースの破断伸びの間にはよい相関が得られた。シース材の劣化がケーブルの劣化を支配するとき、本装置によって電線・ケーブルの劣化を非破壊で求めることができる。
八木 敏明; 森田 洋右; 川上 和市郎; 神村 誠二*; 柳生 秀樹*; 望月 修*; 大西 隆雄*
EIM-90-124, p.65 - 74, 1990/12
原子力発電所にとって重要な電線・ケーブルを非破壊的に診断する方法および測定装置の検討を行った。ケーブル試料に周期的なねじり歪を与え、それに応じたトルクを測定する装置を試作し、熱および逐次劣化(放射線熱)した600V級低圧CVケーブルのトルク値と機械的特性の関係を調べた。ケーブル試料に与える歪に応じたトルク値の大きさは試料の硬さや柔らかさの程度によって変化する。本装置で求めたトルクの値と劣化ケーブルのシース材の破断伸びの間にはよい相関性が得られた。シース材の劣化がケーブルの劣化を支配するとき、本方法(歪-トルク応答)によって、電線・ケーブルの劣化状態を非破壊で定量的に求めることが出来る。
藤原 悟; 荒木 克哉*; 松尾 龍人; 八木 寿梓*; 山田 武*; 柴田 薫; 望月 秀樹*
no journal, ,
A protein -synuclein (-Syn), which is involved with pathogenesis of a neuro-degenerative disorder, Parkinson's disease, forms amyloid fibrils. Propensity for amyloid fibril formation depends on environmental conditions such as pH. We employed neutron scattering to investigate the "dynamic" behavior of -Syn at low and neutral pH, to investigate the relationship between the dynamics and propensity for amyloid fibril formation. We carried out the quasielastic neutron scattering experiments using a high energy resolution near-backscattering spectrometer, BL02 (DNA), at MLF/J-PARC, Japan. Analysis of the quasielasitc scattering spectra showed the increased flexibility of -Syn at low pH. Since the increased flexibility is likely to arise from a wider distribution of conformational substates of -Syn, the results obtained suggest an entropy-driven mechanism of the amyloid fibril formation.
藤原 悟; 荒木 克哉*; 松尾 龍人; 八木 寿梓*; 山田 武*; 柴田 薫; 望月 秀樹*
no journal, ,
A protein -synuclein (-Syn) forms amyloid fibrils. This abnormal protein aggregation is related to pathogenesis of a neuro-degenerative disorder, Parkinson's disease. Propensity for amyloid fibril formation depends on environmental conditions such as pH. We carried out quasielastic neutron scattering experiments to investigate the "dynamic" behavior of -Syn to investigate the relationship between the dynamics and propensity for amyloid fibril formation. The measurements on the solution samples of -Syn in different pH were carried out using a high energy resolution near-backscattering spectrometer, BL02 (DNA), at MLF/J-PARC, Japan. Differences in flexibility of the protein were detected between the different conditions. Since the difference in flexibility is likely to arise from different distributions of conformational substates of -Syn, the results obtained suggest an entropy-driven mechanism of the amyloid fibril formation.
藤原 悟; 荒木 克哉*; 松尾 龍人; 八木 寿梓*; 山田 武*; 柴田 薫; 望月 秀樹*
no journal, ,
The protein, -synuclein (-Syn) forms amyloid fibrils. Formation of amyloid fibrils is associated with the pathogenesis of a neuro-degenerative disorder, Parkinson's disease. In order to obtain insights into the role of the protein dynamics in the mechanism of amyloid fibril formation, we carried out quasielastic neutron scattering experiments and characterized the "dynamic" behavior of -Syn. The measurements on the solution samples of -Syn in the monomeric and fibril states were carried out using a high energy resolution near-backscattering spectrometer, BL02 (DNA), at MLF/J-PARC, Japan. Differences in the dynamical behavior of the protein were detected between the monomeric and fibril states. Analysis of the spectra obtained suggested an entropy-driven mechanism of amyloid fibril formation.