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Amyloid Fibrils

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Related Experiment Video

Updated: May 28, 2026

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

A soluble α-synuclein construct forms a dynamic tetramer.

Wei Wang1, Iva Perovic, Johnathan Chittuluru

  • 1Department of Biochemistry and Molecular Biology, and Stark Neurosciences Research Institute, Indiana University School of Medicine, Indianapolis, IN 46202, USA.

Proceedings of the National Academy of Sciences of the United States of America
|October 19, 2011
PubMed
Summary
This summary is machine-generated.

Parkinson disease-associated protein alpha-synuclein (α-synuclein) forms stable tetramers without lipids. This oligomeric structure, characterized by helical elements and a hydrophobic core, provides insights into Parkinson

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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

Related Experiment Videos

Last Updated: May 28, 2026

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Parkinson disease is linked to the protein alpha-synuclein (α-synuclein).
  • α-synuclein's native structure and oligomeric states are crucial for its function and aggregation.
  • Understanding α-synuclein oligomerization is key to deciphering Parkinson disease pathogenesis.

Purpose of the Study:

  • To investigate the structural properties of a heterologously expressed α-synuclein variant.
  • To determine the oligomeric state and stability of α-synuclein in the absence of membrane interactions.
  • To propose a structural model for the α-synuclein tetramer.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy for sequential assignments and NOE analysis.
  • Circular Dichroism (CD) spectroscopy for secondary structure determination.
  • Total phosphorus analysis, chemical cross-linking, electron microscopy, and thermal unfolding experiments.

Main Results:

  • A 10-residue N-terminally extended α-synuclein forms a stable tetramer independent of lipids.
  • NMR and CD data suggest transient α-helix formation in the N-terminal 100 residues.
  • Electron microscopy reveals a symmetric oligomer with three- or fourfold symmetry.
  • Thermal unfolding indicates the presence of a hydrophobic core within the tetramer.

Conclusions:

  • The α-synuclein tetramer represents a distinct, stable oligomeric state.
  • The tetramer structure is characterized by helical elements and a hydrophobic core, suggesting a dynamic model.
  • This finding provides a structural basis for understanding α-synuclein's behavior in solution and its role in Parkinson disease.