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Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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...

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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
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

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
PubMed
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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Related Experiment Videos

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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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

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.