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Updated: Jun 12, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
The evolving role of solid state nuclear magnetic resonance methods in studies of amyloid fibrils
1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Abstract:
Beginning in the 1990s, solid state nuclear magnetic resonance (ssNMR) methods played a major role in elucidating the molecular structures and properties of amyloid fibrils. General principles that explain these structures and properties were uncovered and experimentally-based structural models were first developed from ssNMR data. Since 2017, cryogenic electron microscopy (cryo-EM) techniques have become capable of solving amyloid structures at near-atomic resolution. Although cryo-EM measurements are now the main approach for structural studies of amyloid fibrils, ssNMR measurements remain essential for studies of certain structures and structural features, as well as studies of dynamical and mechanistic aspects. Recent publications from various research groups illustrate the continuing importance of ssNMR and the unique information available from ssNMR measurements in amyloid research.
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