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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Folding01:22

Protein Folding

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Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
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Related Experiment Video

Updated: May 14, 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

The dynamic structure of α-synuclein multimers.

Thomas Gurry1, Orly Ullman, Charles K Fisher

  • 1Computational and Systems Biology Initiative, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139-4307, USA.

Journal of the American Chemical Society
|February 13, 2013
PubMed
Summary

Alpha-synuclein, implicated in Parkinson's disease, exists as disordered monomers or structured multimers. This study reveals a dynamic ensemble including helical and beta-strand oligomers, reconciling prior observations.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Last Updated: May 14, 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
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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Alpha-synuclein aggregation is central to Parkinson's disease pathogenesis.
  • Monomeric alpha-synuclein is intrinsically disordered, but can form soluble multimers in vivo.
  • Contradictory findings exist regarding helical versus beta-strand rich alpha-synuclein species.

Purpose of the Study:

  • To investigate the diverse multimeric states of alpha-synuclein.
  • To reconcile conflicting observations on alpha-synuclein structure in cellular environments.
  • To understand the role of different alpha-synuclein conformations in aggregation.

Main Methods:

  • Generation of an alpha-synuclein construct with an N-terminal extension.
  • Utilized Nuclear Magnetic Resonance (NMR) chemical shifts.
  • Employed residual dipolar couplings (RDCs) to guide ensemble construction.

Main Results:

  • The dominant state observed is a disordered monomer.
  • A small fraction of helical trimers and tetramers were detected.
  • Trimeric and tetrameric oligomers rich in beta-strand content were also identified.
  • The ensemble provides a structural basis for both helical and beta-strand forms.

Conclusions:

  • The findings reconcile the presence of both disordered monomers and helical tetramers in cells.
  • Helical tetramers may act as a storage form of alpha-synuclein at high concentrations.
  • This storage mechanism could prevent aggregation of non-membrane-bound monomers.
  • Understanding these states is crucial for Parkinson's disease research.