Journal
CHEMBIOCHEM
Volume 10, Issue 3, Pages 436-+Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.200800644
Keywords
fluorescence spectroscopy; intrinsic disorder; protein folding; single-molecule studies; synuclein
Funding
- Stichting Internationaal Parkinson Fonds
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO)
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Upon interaction with SIDS, 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 SIDS 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.
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