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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: May 10, 2026

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells
14:12

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells

Published on: December 11, 2021

Quantitative fluorescence co-localization to study protein-receptor complexes.

Shanica N Pompey1, Peter Michaely, Katherine Luby-Phelps

  • 1Department of Cell Biology, UT Southwestern Medical School, Dallas, TX, USA.

Methods in Molecular Biology (Clifton, N.J.)
|June 5, 2013
PubMed
Summary
This summary is machine-generated.

Fluorescence microscopy enables quantitative assessment of molecular interactions through co-localization analysis. This technique visualizes where tagged molecules overlap, supporting evidence of their interaction within cells.

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Last Updated: May 10, 2026

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells
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Published on: December 11, 2021

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Bimolecular Fluorescence Complementation
08:54

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

Area of Science:

  • Cell Biology
  • Microscopy Techniques
  • Biochemistry

Background:

  • Co-localization analysis using fluorescence microscopy quantifies molecular interactions.
  • It involves tagging interacting molecules with distinct fluorophores for visualization.

Purpose of the Study:

  • To detail quantitative co-localization analysis for studying molecular interactions.
  • To provide a protocol for time-dependent co-localization of lipoproteins with LDLR and EEA1.

Main Methods:

  • Labeling interacting partners with different fluorophores (e.g., direct labeling, fluorescent constructs, immunofluorescence).
  • Acquiring two-channel digital images and performing pixel-wise intensity comparisons.
  • Utilizing image segmentation to identify overlapping regions above background noise.

Main Results:

  • Co-localization analysis reveals spatial overlap of tagged molecules.
  • Quantitative metrics assess the degree and significance of co-localization.
  • Image maps visualize the distribution of co-localized pixels.

Conclusions:

  • Co-localization analysis supports the inference of molecular interactions within cells.
  • Software solutions simplify segmentation and metric calculation for co-localization studies.
  • The described protocol facilitates studying dynamic molecular interactions.