Selective observation of semi-rigid non-core residues in dynamically complex mutant huntingtin protein fibrils
Many amyloid-forming proteins, which are normally intrinsically disordered, undergo a disorder-to-order transition to form fibrils with a rigid β-sheet core flanked by disordered domains. Solid-state NMR (ssNMR) and cryogenic electron microscopy (cryoEM) excel at resolving the rigid structures withi...
| Main Authors: | , , |
|---|---|
| 格式: | Article |
| 語言: | English |
| 出版: |
Elsevier
2022-01-01
|
| 叢編: | Journal of Structural Biology: X |
| 主題: | |
| 在線閱讀: | http://www.sciencedirect.com/science/article/pii/S2590152422000186 |