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Related Concept Videos

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...

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Related Experiment Video

Updated: Jun 5, 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

A Bayesian method for single molecule, fluorescence burst analysis.

P R Barber, S M Ameer-Beg, S Pathmananthan

    Biomedical Optics Express
    |January 25, 2011
    PubMed
    Summary
    This summary is machine-generated.

    This study introduces a Bayesian method for identifying single-molecule fluorescence bursts, crucial for analyzing molecular dynamics and environmental conditions without ensemble averaging artifacts. The new approach successfully detects low-amplitude bursts and estimates fluorescence lifetime.

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    Related Experiment Videos

    Last Updated: Jun 5, 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

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    High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy
    15:13

    High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy

    Published on: July 25, 2014

    Area of Science:

    • Biophysics
    • Analytical Chemistry
    • Physical Chemistry

    Background:

    • Single-molecule analysis offers insights into molecular dynamics and environmental conditions, overcoming limitations of ensemble averaging.
    • Identifying weak fluorescent bursts from single molecules in experiments like burst integrated fluorescence lifetime (BIFL) is a significant challenge.
    • Accurate determination of physical parameters like fluorescence lifetime is essential for understanding molecular behavior.

    Purpose of the Study:

    • To develop a robust Bayesian method for identifying single-molecule fluorescence bursts in experimental data.
    • To demonstrate the capability of the method in detecting low-amplitude signal bursts.
    • To accurately estimate fluorescence lifetime and its associated error from detected burst data.

    Main Methods:

    • A Bayesian approach based on model selection was employed for burst identification.
    • The method was tested for its ability to detect bursts with signal amplitudes as low as 10% of the total amplitude.
    • Fluorescence lifetime and its error were estimated directly from the identified burst data.

    Main Results:

    • The developed Bayesian method effectively identifies single-molecule fluorescence bursts.
    • The method successfully detected bursts with a signal amplitude of 10%.
    • Accurate estimation of fluorescence lifetime and its error from burst data was achieved.

    Conclusions:

    • The Bayesian burst identification method provides a reliable tool for single-molecule fluorescence analysis.
    • This technique enables the study of molecular interactions, dynamics, and sub-species with improved sensitivity.
    • The method overcomes a key challenge in burst integrated fluorescence lifetime (BIFL) experiments, enhancing data analysis capabilities.