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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...
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.
Sorting of outer membrane proteins:
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,...
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...

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Updated: Jun 16, 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

Dynamic transitions of membrane-active peptides.

Stephan L Grage1, Sergii Afonin, Anne S Ulrich

  • 1Karlsruhe Institute of Technology, Institute for Biological Interfaces (IBG-2), Institute of Organic Chemistry, Karlsruhe, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|January 23, 2010
PubMed
Summary

Membrane-active peptides dynamically change their orientation and oligomeric state within cell membranes. These adaptable interactions are crucial for diverse biological functions, including host defense and membrane fusion.

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Last Updated: Jun 16, 2026

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

Published on: December 19, 2020

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
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Published on: June 28, 2019

Measuring Peptide Translocation into Large Unilamellar Vesicles
12:27

Measuring Peptide Translocation into Large Unilamellar Vesicles

Published on: January 27, 2012

Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • Membrane-active peptides are vital for cellular processes like fusion and host defense.
  • Peptide interaction with lipid bilayers depends on factors like orientation and oligomerization.

Purpose of the Study:

  • To explore the versatile interaction modes of membrane-active peptides with lipid bilayers.
  • To understand how environmental factors influence peptide states and biological activity.

Main Methods:

  • Analysis of peptide-lipid interactions in model membrane systems.
  • Investigating changes in peptide orientation and oligomerization.
  • Examining environmental influences such as peptide concentration, temperature, lipid composition, and pH.

Main Results:

  • Peptides exhibit multiple alignments and oligomeric states, not a single fixed mode.
  • Antimicrobial peptides transition from surface-parallel to transmembrane states with increasing concentration.
  • Environmental factors like temperature, lipid composition, and pH induce shifts in peptide states.

Conclusions:

  • Membrane-active peptides can transition between different states (orientation, oligomerization) in response to environmental changes.
  • These dynamic transitions are driven by altered peptide-peptide and peptide-lipid interactions.
  • The ability to change states is fundamental to the biological activities of these peptides in both model and native biomembranes.