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Updated: Aug 2, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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高分辨率的Aβ42粉样纤维的结构特征通过魔法角度旋转NMR

Michael T Colvin1, Robert Silvers1, Birgitta Frohm2

  • 1†Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.

Journal of the American Chemical Society
|May 23, 2015
PubMed
概括

研究人员描述了粉样β 1-42 (Aβ1-42) 纤维,这是阿尔茨海默病的关键组成部分. 通过使用先进的NMR,他们发现了一种单一的纤维结构,具有动态的N-终端残留物和稳定的核心,为AD病原体提供了洞察力.

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相关概念视频

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...