Related Experiment Video
Updated: Jun 22, 2026
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
Structural characterization of alpha-synuclein in an aggregation prone state.
Min-Kyu Cho1, Gabrielle Nodet, Hai-Young Kim
1Department for NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Protein Science : a Publication of the Protein Society
|June 26, 2009
Summary
Alpha-synuclein (alphaS) remains unfolded at acidic pH but shows altered structural properties. This aggregation-prone state may offer insights into Parkinson's disease pathogenesis.
Area of Science:
- Biochemistry
- Neuroscience
- Structural Biology
Background:
- Alpha-synuclein aggregation is linked to Parkinson's disease.
- The specific pathogenic species and its molecular characteristics remain elusive.
Purpose of the Study:
- To investigate the structural properties of alpha-synuclein (alphaS) in an aggregation-prone state.
- To understand alphaS behavior at acidic pH using NMR spectroscopy and computational methods.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy.
- Computational modeling.
- Study of alphaS structural properties at acidic pH.
Main Results:
- Alpha-synuclein remains natively unfolded at acidic pH.
- Secondary structure propensities change near acidic residues.
- The C-terminal region rigidifies and compacts.
- Increased proximity between the NAC-region and C-terminal region observed.
- Decreased probability of N- and C-terminal region interactions.
Conclusions:
- Acidic pH induces specific conformational changes in alphaS.
- These structural alterations in alpha-synuclein may be relevant to Parkinson's disease.
- Further research into aggregation-prone states is crucial for understanding neurodegenerative mechanisms.
More Related Videos
Related Concept Videos
03:03Amyloid 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 deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid 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 deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:22Protein Folding
Overview
01:25Protein 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 Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
01:13Protein Organization
Overview
02:15Protein 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...
A protein's shape is critical to its function. For example, an enzyme can...