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

Authors

  • Gertjan Veldhuis Dr.,

    1. Biophysical Engineering Group, MESA+ Institute for Nanotechnology and Institute for Biomedical Technology, University of Twente, P. O. Box 217, 7500 AE, Enschede (The Netherlands), Fax: (+31) 53-489-1105
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  • Ine Segers-Nolten Dr.,

    1. Biophysical Engineering Group, MESA+ Institute for Nanotechnology and Institute for Biomedical Technology, University of Twente, P. O. Box 217, 7500 AE, Enschede (The Netherlands), Fax: (+31) 53-489-1105
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  • Eva Ferlemann,

    1. Biophysical Engineering Group, MESA+ Institute for Nanotechnology and Institute for Biomedical Technology, University of Twente, P. O. Box 217, 7500 AE, Enschede (The Netherlands), Fax: (+31) 53-489-1105
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  • Vinod Subramaniam Prof. Dr.

    1. Biophysical Engineering Group, MESA+ Institute for Nanotechnology and Institute for Biomedical Technology, University of Twente, P. O. Box 217, 7500 AE, Enschede (The Netherlands), Fax: (+31) 53-489-1105
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Abstract

SDS-concentration-dependent α-synuclein structure: Upon interaction with SDS, αSyn folds into a structure with two antiparallel α-helices. We show from single-molecule FRET that αSynn 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.

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