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• W2053203978 abstract "SDS-concentration-dependent α-synuclein structure: Upon interaction with SDS, αSyn folds into a structure with two antiparallel α-helices. We show from single-molecule FRET that αSynn adopts this conformation in an all-or-none fashion below the SDS critical micelle concentration. Population of the folded species is directly coupled to an increase in α-helix content; this suggests that the entire N terminus is involved in the transaction." @default.
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• W2053203978 date "2009-02-13" @default.
• W2053203978 modified "2023-09-27" @default.
• W2053203978 title "Single-Molecule FRET Reveals Structural Heterogeneity of SDS-Bound α-Synuclein" @default.
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• W2053203978 doi "https://doi.org/10.1002/cbic.200800644" @default.
• W2053203978 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19107759" @default.
• W2053203978 hasPublicationYear "2009" @default.
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