Dynamics of Amyloid β Fibrils Revealed by Solid-state NMR
Dynamics of Amyloid β Fibrils Revealed by Solid-state NMR
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DOI：
10.1074/jbc.m111.308619
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发表时间：
2012-01-13
影响因子：
4.8
通讯作者：
Huster, Daniel
中科院分区：
文献类型：
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作者：
Scheidt, Holger A.;Morgado, Isabel;Huster, Daniel
我们已经研究了使用固态核磁共振光谱学的成熟淀粉样蛋白β（A β）原纤维的位点特异性骨架动力学。总体而言，已知的β-折叠片段和连接这两条β-链的转角表现出0.8至0.95的高阶参数，表明低构象柔性。前约8个N-末端残基和最后的C-末端残基表现出类似于0.4和0.8之间的低阶参数。有趣的是，前两个残基Asp（1）和Ala（2）的序参数再次增加，表明N端可能具有一定的结构重要性。
We have investigated the site-specific backbone dynamics of mature amyloid beta (A beta) fibrils using solid-state NMR spectroscopy. Overall, the known beta-sheet segments and the turn linking these two beta-strands exhibit high order parameters between 0.8 and 0.95, suggesting low conformational flexibility. The first approximately eight N-terminal and the last C-terminal residues exhibit lower order parameters between similar to 0.4 and 0.8. Interestingly, the order parameters increase again for the first two residues, Asp(1) and Ala(2), suggesting that the N terminus could carry some structural importance.