Supplementary Figure 6: Comparison of the Cα chemical-shift perturbations for three early-onset Parkinson's disease–mutant forms of α-syn, relative to the wild-type chemical shifts. | Nature Structural & Molecular Biology

Supplementary Figure 6: Comparison of the Cα chemical-shift perturbations for three early-onset Parkinson's disease–mutant forms of α-syn, relative to the wild-type chemical shifts.

From: Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

Supplementary Figure 6

(a–c) Chemical shift perturbation plots of the absolute deviation of the Cα shifts for A30P, E46K, and A53T previously published (Lemkau, L.R. et al. Mutant protein A30P α-synuclein adopts wild-type fibril structure, despite slower fibrillation kinetics. J. Biol. Chem. 287, 11526-11532 (2012); Lemkau, L.R. et al. Site-specific perturbations of α-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46K. PLoS One 8, e49750 (2013).) relative to the wild-type chemical shifts used in this work.

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