title: Single-molecule FRET reveals structural heterogeneity of SDS-bound alpha-synuclein.
abstract: SDS-concentration-dependent alpha-synuclein structure: Upon interaction with SDS, alpha Syn folds into a structure with two antiparallel alpha-helices. We show from single-molecule FRET that alpha 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 alpha-helix content; this suggests that the entire N terminus is involved in the transaction.
authors.affiliation: Biophysical Engineering Group, MESA+ Institute for Nanotechnology and Institute for Biomedical Technology, University of Twente, Enschede, The Netherlands.
authors.forename: Gertjan
authors.initials: G
authors.lastname: Veldhuis
authors.forename: Ine
authors.initials: I
authors.lastname: Segers-Nolten
authors.forename: Eva
authors.initials: E
authors.lastname: Ferlemann
authors.forename: Vinod
authors.initials: V
authors.lastname: Subramaniam
mesh_terms: D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry* / Q000378:metabolism; D013501:Surface-Active Agents / Q000737:chemistry* / Q000378:metabolism; D051844:alpha-Synuclein / Q000737:chemistry* / Q000378:metabolism
chemical_list: D013501:Surface-Active Agents; D051844:alpha-Synuclein; D012967:Sodium Dodecyl Sulfate