Single-Molecule FRET Reveals Structural Heterogeneity of SDS-Bound α-Synuclein

Share/Save/Bookmark

Veldhuis, Gertjan and Segers-Nolten, Ine and Ferleman, Eva and Subramaniam, Vinod (2008) Single-Molecule FRET Reveals Structural Heterogeneity of SDS-Bound α-Synuclein. ChemBioChem, 10 (3). pp. 436-439. ISSN 1439-4227

[img] PDF
Restricted to UT campus only
: Request a copy
456kB
Abstract: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.
Item Type:Article
Copyright:© 2008 Wiley
Faculty:
Science and Technology (TNW)
Research Group:
Link to this item:http://purl.utwente.nl/publications/72559
Official URL:http://dx.doi.org/10.1002/cbic.200800644
Export this item as:BibTeX
EndNote
HTML Citation
Reference Manager

 

Repository Staff Only: item control page

Metis ID: 251639