Single-molecule FRET reveals structural heterogeneity of SDS-bound alpha-synuclein

Gertjan Veldhuis, Ine Segers-Nolten, Eva Ferlemann, Vinod Subramaniam

    Research output: Contribution to JournalArticleAcademicpeer-review

    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 languageEnglish
    Pages (from-to)436-9
    Number of pages4
    JournalChemBioChem
    Volume10
    Issue number3
    DOIs
    Publication statusPublished - 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

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