Single-molecule FRET reveals structural heterogeneity of SDS-bound alpha-synuclein.
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.
Veldhuis
Gertjan
G
Biophysical Engineering Group, MESA+ Institute for Nanotechnology and Institute for Biomedical Technology, University of Twente, Enschede, The Netherlands.
Segers-Nolten
Ine
I
Ferlemann
Eva
E
Subramaniam
Vinod
V
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
D013501:Surface-Active Agents; D051844:alpha-Synuclein; D012967:Sodium Dodecyl Sulfate