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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
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Published on: May 30, 2021

Explaining the structural plasticity of α-synuclein.

Orly Ullman1, Charles K Fisher, Collin M Stultz

  • 1Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139-4307, USA.

Journal of the American Chemical Society
|October 28, 2011
PubMed
Summary
This summary is machine-generated.

Monomeric alpha-synuclein exhibits structural plasticity, adopting conformations that can lead to aggregation or form helical tetramers. Understanding this protein

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Last Updated: May 28, 2026

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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

Area of Science:

  • Structural Biology
  • Neurodegenerative Diseases
  • Protein Misfolding

Background:

  • Alpha-synuclein (α-synuclein) is implicated in neurodegenerative disorders.
  • Monomeric α-synuclein is intrinsically disordered but can adopt various structures, including aggregates and helical segments.
  • Understanding α-synuclein's structural plasticity is crucial for deciphering its role in disease pathogenesis.

Purpose of the Study:

  • To elucidate the physical basis of α-synuclein's structural plasticity.
  • To characterize the ensemble of monomeric α-synuclein conformations.
  • To investigate the relationship between different structural states and aggregation propensity.

Main Methods:

  • Generated an ensemble for monomeric α-synuclein using Bayesian formalism.
  • Integrated data from Nuclear Magnetic Resonance (NMR) chemical shifts, Residual Dipolar Couplings (RDCs), and Small-Angle X-ray Scattering (SAXS).
  • Combined experimental data with molecular simulations.

Main Results:

  • A fraction of the ensemble shows the aggregation-prone NAC(8-18) segment in a solvent-exposed, extended conformation capable of forming cross-β structure.
  • A significant portion of structures exhibits long-range contacts between the N- and C-termini, with some also exposing the NAC(8-18) segment.
  • The study identified α-synuclein conformations with amphipathic helices capable of self-association into tetrameric structures.

Conclusions:

  • The unfolded ensemble of monomeric α-synuclein provides a comprehensive view of its conformational landscape.
  • Specific conformations, including solvent-exposed NAC(8-18) segments and N-/C-terminal contacts, contribute to α-synuclein's aggregation propensity.
  • The findings explain how monomeric α-synuclein can transition into different functional or pathological structures.