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-synuclein studied by quasielastic neutron scattering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：64.99(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.
川崎 克也; 望月 薫*; 鈴木 武彦; 木内 伸幸
JAERI-Tech 2004-070, 50 Pages, 2004/12
JAERI-Tech-2004-070.pdf:18.19MB
放射線管理用試料集中計測システムは、日本原子力研究所東海研究所の施設及び環境の放射線管理に必要な多種多数の試料について、測定及びデータ解析を集中的に行うものであり、1981年度から本格的な運用を開始し現在では年間2万件を超える測定に使われている。本システムの中枢をなすコンピュータは、機器の老朽化が進むとともに、メーカーサポートの終了が相次いだことから、安定な運用に支障が生じてきた。そこで、2003年度にコンピュータ関連機器の更新とシステムの再構築を行った。今回の更新では、コンピュータのハードウェア構成を、データサーバとパーソナルコンピュータの複合型のクライアントサーバーシステムとした。また、ソフトウェアには、試料情報登録用にイントラネットワークを利用したWeb方式を新たに導入し、さらに、依頼試料に対する進捗状況の確認及び結果の閲覧を、利用者自身のパーソナルコンピュータからオンラインで直接行える機能も新たに追加した。この結果、利用者の利便性をさらに広げることができた。
藤井 克年; 高橋 照彦; 三枝 純; 宍戸 宣仁; 望月 薫*; 野嶋 峻; 秋山 勇; 清水 勇
no journal, ,
NSRRは反応度事故を模擬したパルス状の出力を発生させる運転を行っている。放射線管理上、このパルス運転時の漏えい線量は中性子サーベイメータ(レムカウンタ)を用いて測定しているが、パルス運転時のように狭い時間範囲に大量の中性子がレムカウンタで検出される場合、測定値は数え落としの補正が必要となる。今回、放射線管理の観点から実用的な補正係数の算出を目的とし、数え落としについて実験的に検証した。検証の方法として、マヒ型モデルを想定したシミュレーション計算値と実験による測定値の比較を行った。シミュレーションに用いた不感時間は、2線源法及び線源-パルサー法により評価した。シミュレーション計算は、実験による測定結果をよく再現しており、本実験のような高計数率の領域においても数え落としをよく評価できた。この結果から、原子炉出力に応じた補正係数の算出が可能となった。
-synuclein and its relation to propensity for 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), 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.
-synuclein; Implication for propensity for 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.
-synuclein detected by neutron scattering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.
