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

G. Veldhuis; G.J. Veldhuis; Gezina M.J. Segers-Nolten; Eva Ferleman; Vinod Subramaniam

doi:10.1002/cbic.200800644

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

G. Veldhuis
, G.J. Veldhuis
, Gezina M.J. Segers-Nolten
, Eva Ferleman
, Vinod Subramaniam

Research output: Contribution to journal › Article › Academic › peer-review

50 Citations (Scopus)

10 Downloads (Pure)

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.

Original language	Undefined
Pages (from-to)	-
Journal	ChemBioChem
Volume	10
Issue number	3
DOIs	https://doi.org/10.1002/cbic.200800644
Publication status	Published - 2008

Keywords

Synuclein
intrinsic disorder
single-molecule studies
Fluorescence spectroscopy
IR-72559
METIS-251639
protein folding

Access to Document

10.1002/cbic.200800644

Cite this

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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.",

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AU - Ferleman, Eva

AU - Subramaniam, Vinod

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KW - Synuclein

KW - intrinsic disorder

KW - single-molecule studies

KW - Fluorescence spectroscopy

KW - IR-72559

KW - METIS-251639

KW - protein folding

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