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Updated: Jul 14, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Magnetic resonance in the solid state: applications to protein folding, amyloid fibrils and membrane proteins
1Solid-state NMR, Max-Planck-Institut für Biophysikalische Chemie, 37077 Göttingen, Germany. maba@mpibpc.mpg.de
Abstract:
Solid-state nuclear magnetic resonance (ssNMR) represents a spectroscopic method to study non-crystalline molecules at atomic resolution. Advancements in spectroscopy and biochemistry provide increasing possibilities to study structure and dynamics of complex biomolecular systems by ssNMR. Here, methodological aspects and applications in the context of protein folding and aggregation are discussed. In addition, studies involving membrane proteins are considered.
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