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

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

doi:10.1002/cbic.200800644

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

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

Research output: Contribution to Journal › Article › Academic › peer-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 language	English
Pages (from-to)	436-9
Number of pages	4
Journal	ChemBioChem
Volume	10
Issue number	3
DOIs	https://doi.org/10.1002/cbic.200800644
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

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title = "Single-molecule FRET reveals structural heterogeneity of SDS-bound alpha-synuclein",

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.",

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",

author = "Gertjan Veldhuis and Ine Segers-Nolten and Eva Ferlemann and Vinod Subramaniam",

year = "2009",

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doi = "10.1002/cbic.200800644",

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T1 - Single-molecule FRET reveals structural heterogeneity of SDS-bound alpha-synuclein

AU - Veldhuis, Gertjan

AU - Segers-Nolten, Ine

AU - Ferlemann, Eva

AU - Subramaniam, Vinod

PY - 2009/2/13

Y1 - 2009/2/13

N2 - 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.

AB - 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.

KW - Fluorescence Resonance Energy Transfer

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Protein Conformation

KW - Sodium Dodecyl Sulfate

KW - Surface-Active Agents

KW - alpha-Synuclein

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1002/cbic.200800644

DO - 10.1002/cbic.200800644

M3 - Article

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SN - 1439-4227

VL - 10

SP - 436

EP - 439

JO - ChemBioChem

JF - ChemBioChem

IS - 3

ER -

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

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