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Updated: Jun 22, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Solid-state NMR backbone chemical shift assignments of α-synuclein amyloid fibrils at fast MAS regime
Zigmantas Toleikis1,2, Piotr Paluch3, Ewelina Kuc3
1Latvian Institute of Organic Synthesis, Aizkraukles 21, Riga, LV-1006, Latvia.
Abstract:
The α-synuclein (α-syn) amyloid fibrils are involved in various neurogenerative diseases. Solid-state NMR (ssNMR) has been showed as a powerful tool to study α-syn aggregates. Here, we report the 1H, 13C and 15N back-bone chemical shifts of a new α-syn polymorph obtained using proton-detected ssNMR spectroscopy under fast (95 kHz) magic-angle spinning conditions. The manual chemical shift assignments were cross-validated using FLYA algorithm. The secondary structural elements of α-syn fibrils were calculated using 13C chemical shift differences and TALOS software.
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