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Related Concept Videos

Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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 17, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

Membrane translocation assayed by fluorescence spectroscopy.

Jana Broecker1, Sandro Keller

  • 1Leibniz Institute of Molecular Pharmacology FMP, Berlin, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|December 17, 2009
PubMed
Summary
This summary is machine-generated.

This study presents a simple fluorescence spectroscopy method to track how molecules like peptides and proteins cross lipid membranes. This technique is fast, cost-effective, and useful for liposome research.

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Related Experiment Videos

Last Updated: Jun 17, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
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Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

From Fast Fluorescence Imaging to Molecular Diffusion Law on Live Cell Membranes in a Commercial Microscope
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Published on: October 9, 2014

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

Area of Science:

  • Biochemistry
  • Biophysics
  • Membrane Biology

Background:

  • Assessing biomolecule and drug translocation across lipid membranes is crucial for basic research and liposome applications.
  • Lipid membrane permeability is key for drug delivery and understanding cellular processes.
  • Receptor-independent membrane crossing is a significant challenge in drug development.

Purpose of the Study:

  • To present a powerful, straightforward, and inexpensive method for monitoring membrane translocation.
  • To enable the assessment of biomolecules and drugs crossing lipid membranes without receptors.
  • To provide a practical approach for studying liposome-mediated delivery.

Main Methods:

  • Utilizing steady-state fluorescence spectroscopy.
  • Employing a combination of uptake, release, and dilution experiments.
  • Leveraging intrinsic tryptophan fluorescence in peptides and proteins, avoiding extrinsic labeling.

Main Results:

  • Demonstrated a reliable method for monitoring membrane translocation of fluorescent compounds.
  • Showcased the effectiveness of the technique for peptides and proteins with intrinsic tryptophan.
  • Validated a rapid experimental workflow, completable within two days.

Conclusions:

  • Fluorescence spectroscopy offers a powerful tool for studying receptor-independent membrane translocation.
  • The described method is efficient and cost-effective for both research and liposome applications.
  • Intrinsic fluorescence simplifies the study of peptide and protein membrane interactions.