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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell types have...
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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
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Related Experiment Video

Updated: May 8, 2026

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide
07:33

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Published on: December 19, 2020

Peptide interaction with and insertion into membranes.

Ron Saar-Dover1, Avraham Ashkenazi, Yechiel Shai

  • 1Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.

Methods in Molecular Biology (Clifton, N.J.)
|September 3, 2013
PubMed
Summary
This summary is machine-generated.

This study introduces spectroscopic methods using fluorescently labeled peptides to analyze peptide-membrane interactions and peptide-peptide assembly within lipid bilayers, offering insights into molecular behavior.

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Last Updated: May 8, 2026

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide
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Published on: December 19, 2020

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10:26

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Area of Science:

  • Biophysics
  • Membrane Biology
  • Biochemistry

Background:

  • Membrane-active peptides and protein fragments interact with cellular membranes.
  • These interactions can lead to peptide insertion and assembly within the lipid bilayer.

Purpose of the Study:

  • To develop and apply spectroscopic techniques for quantifying peptide-membrane and peptide-peptide interactions.
  • To investigate the behavior of peptides within lipid bilayers using fluorescent probes.

Main Methods:

  • Utilizing NBD (N-phenyl-1-naphthylamine) and rhodamine fluorescently labeled peptides.
  • Employing spectroscopic approaches to monitor peptide-membrane and peptide-peptide interactions.
  • Leveraging the distinct physical properties of NBD and rhodamine in solution and membrane environments.

Main Results:

  • Demonstrated the capability of spectroscopic methods to measure peptide-membrane interactions.
  • Showcased the ability to detect peptide-peptide interactions and assembly within the membrane.
  • Provided insights into the interplay between peptides and lipids based on probe behavior.

Conclusions:

  • Spectroscopic analysis with NBD and rhodamine labeled peptides is effective for studying peptide-membrane and within-membrane interactions.
  • The physical properties of these fluorescent probes offer valuable data on peptide-lipid dynamics.
  • This approach enhances understanding of molecular mechanisms governing peptide behavior in biological membranes.