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 a-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 a-syn fibrils were calculated using ¹³C chemical shift differences and TALOS software.
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Toleikis et al. (2024) studied this question.
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