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Related Experiment Video

Updated: May 18, 2026

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

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

Published on: May 30, 2021

Function and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule

Adam J Trexler¹, Elizabeth Rhoades

¹Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, P.O. Box 208114, New Haven, CT 06511, USA.

Molecular Neurobiology

|September 18, 2012

Summary

Parkinson's disease involves alpha-synuclein protein aggregation in the brain. Single-molecule fluorescence studies reveal insights into alpha-synuclein

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Last Updated: May 18, 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

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Published on: September 12, 2019

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

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

Published on: June 23, 2022

Area of Science:

Neuroscience
Biochemistry
Biophysics

Background:

Parkinson's disease (PD) is characterized by alpha-synuclein (α-syn) aggregation in the substantia nigra.
Monomeric α-synuclein lacks stable structure and forms complex fibrillar aggregates via intermediate oligomeric species.

Purpose of the Study:

To review single-molecule fluorescence studies of α-synuclein.
To elucidate the role of α-synuclein in Parkinson's disease pathogenesis.

Main Methods:

Review of existing literature on single-molecule fluorescence spectroscopy.
Analysis of studies investigating α-synuclein aggregation dynamics.

Main Results:

Single-molecule techniques are adept at characterizing dynamic and heterogeneous protein samples like α-synuclein.
These studies provide crucial data on the aggregation pathway and oligomeric species involved.

Conclusions:

Single-molecule fluorescence has significantly advanced the understanding of α-synuclein's function and its implications in Parkinson's disease.
Further research using these techniques can deepen insights into PD mechanisms.