Single molecule FRET reveals structural heterogeneity of SDS-bound alpha-synuclein

G. Veldhuis, G.J. Veldhuis, Gezina M.J. Segers-Nolten, Eva Ferleman, Vinod Subramaniam

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SDS-concentration-dependent α-synuclein structure: Upon interaction with SDS, Syn folds into a structure with two antiparallel α-helices. We show from single-molecule FRET that Synn 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.
Original languageUndefined
Pages (from-to)-
Issue number3
Publication statusPublished - 2008


  • Synuclein
  • intrinsic disorder
  • single-molecule studies
  • Fluorescence spectroscopy
  • IR-72559
  • METIS-251639
  • protein folding

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