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.
Original language | English |
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Pages (from-to) | 436-9 |
Number of pages | 4 |
Journal | ChemBioChem |
Volume | 10 |
Issue number | 3 |
DOIs | |
Publication status | Published - 13 Feb 2009 |
Keywords
- Fluorescence Resonance Energy Transfer
- Models, Molecular
- Molecular Sequence Data
- Protein Conformation
- Sodium Dodecyl Sulfate
- Surface-Active Agents
- alpha-Synuclein
- Journal Article
- Research Support, Non-U.S. Gov't