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Related Concept Videos

Fluid Mosaic Model01:19

Fluid Mosaic Model

Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich with the analogy of...
Fluid Mosaic Model01:34

Fluid Mosaic Model

The fluid mosaic model was first proposed as a visual representation of research observations. The model comprises the composition and dynamics of membranes and serves as a foundation for future membrane-related studies. The model depicts the structure of the plasma membrane with a variety of components, which include phospholipids, proteins, and carbohydrates. These integral molecules are loosely bound, defining the cell’s border and providing fluidity for optimal function.LipidsThe most...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

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...
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
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Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Membrane Fluidity01:23

Membrane Fluidity

Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.Fatty acids tails of phospholipids can be either saturated or...

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Related Experiment Video

Updated: Jun 24, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

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Published on: May 26, 2011

Tracking membrane protein association in model membranes.

Myriam Reffay1, Yann Gambin, Houssain Benabdelhak

  • 1Laboratoire de Physique Statistique, Ecole Normale Supérieure, UMR 8550 CNRS-UPMC, Université Paris 06, Paris, France.

Plos One
|April 2, 2009
PubMed
Summary

This study introduces a novel biomimetic sponge phase system to investigate membrane protein interactions. It reveals how MexA and OprM proteins from Pseudomonas aeruginosa form complexes within bilayers, with stoichiometry varying by pH.

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

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Last Updated: Jun 24, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Published on: May 26, 2011

Realistic Membrane Modeling Using Complex Lipid Mixtures in Simulation Studies
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Area of Science:

  • Biochemistry
  • Membrane Biology
  • Biophysics

Background:

  • Membrane proteins are crucial for cellular processes but challenging to study due to their hydrophobic nature.
  • Current methods using detergent-solubilized proteins do not accurately mimic the native 2D membrane environment.
  • Development of biomimetic membrane systems is essential for understanding membrane protein behavior.

Purpose of the Study:

  • To develop and validate a novel biomimetic sponge phase system for studying membrane protein interactions.
  • To investigate the interaction modes, complex formation, and stoichiometry of MexA and OprM proteins from Pseudomonas aeruginosa.
  • To determine the influence of bilayer spacing and pH on protein complex formation.

Main Methods:

  • Utilized a versatile sponge phase system allowing adjustable bilayer spacing.
  • Employed Fluorescence Recovery After fringe Pattern Photobleaching (FRAPP) to analyze protein interactions.
  • Validated the system using the streptavidin-biotinylated peptide complex before studying MexA-OprM.

Main Results:

  • MexA is confirmed to be embedded within the bilayer.
  • MexA and OprM interact only when in opposing bilayers, not laterally within the same bilayer.
  • Maximum complex formation occurs at a bilayer separation of ~200 Å, mimicking periplasmic thickness.
  • MexA-OprM complex stoichiometry is pH-dependent, ranging from 2-6 MexA per OprM trimer as pH decreases from 7.5 to 5.5.
  • Protein association is enhanced by restricted positioning and orientation within bilayers.

Conclusions:

  • The sponge phase system effectively mimics membrane environments for studying protein-protein interactions.
  • The study elucidates the interaction mechanism and pH-dependent stoichiometry of the MexA-OprM complex.
  • This technique provides valuable insights into membrane protein complex geometry and stoichiometry in a near-native state.