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. 2010 May 3;49(20):3469-72.
doi: 10.1002/anie.201000378.

Alteration of the alpha-synuclein folding landscape by a mutation related to Parkinson's disease

Allan Chris M Ferreon  1 , Crystal R Moran, Josephine C Ferreon, Ashok A Deniz
Affiliations
Free PMC article

Alteration of the alpha-synuclein folding landscape by a mutation related to Parkinson's disease

Allan Chris M Ferreon et al. Angew Chem Int Ed Engl. .
Free PMC article
No abstract available

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Figures

Figure 1
Figure 1
Three-state thermal unfolding of WT α-synuclein, the PD-linked A53T and E46K mutants, and a C-terminal-truncation variant (residues 1–107). Protein-denaturation transitions were monitored by far-UV CD spectroscopy in the presence of SDS (1 mm). Unfolding data were collected from 0 to 100°C for all peptides except αSyn 1–107 (0–70°C), which aggregates at higher temperatures under the experimental conditions used (see the Supporting Information for additional details).
Figure 2
Figure 2
Single-molecule and ensemble characterization of the effect of the PD-linked A30P mutation on the coupled binding and folding of α-synuclein. a,b) Thermal unfolding of WT α-synuclein (a) and the A30P mutant (b) bound to SDS monomers, as monitored at the ensemble level by CD spectroscopy in the presence of SDS (1 mm). c) Conformational transitions of A30P α-synuclein induced by changes in ligand concentration at room temperature, as detected at the single-molecule level by smFRET. d) Two-dimensional contour plot of previously reported WT data for comparison with the corresponding plot for the A30P mutant in (e). e) Two-dimensional contour plot of the raw data presented in (c). U, I, and F are different protein conformational states that exhibit characteristic FRET efficiency and helicity. U is the natively unfolded state, I corresponds to a bent helical structure previously solved by NMR spectroscopy (1XQ8), and F is an extended α-helix structure. (See the Supporting Information for additional details).
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