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Related Concept Videos

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

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...
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
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...
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...

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Related Experiment Video

Updated: May 31, 2026

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

Dynamic structure formation of peripheral membrane proteins.

Diana Morozova1, Gernot Guigas, Matthias Weiss

  • 1Cellular Biophysics Group, German Cancer Research Center, Heidelberg, Germany.

Plos Computational Biology
|July 7, 2011
PubMed
Summary

Peripheral membrane proteins form diverse structures through membrane interactions. These protein assemblies are crucial for cellular processes like signaling and transport.

Area of Science:

  • Biophysics
  • Computational Biology
  • Cell Biology

Background:

  • Peripheral membrane proteins interact with lipid bilayers.
  • Understanding protein assembly mechanisms is vital for cell function.

Purpose of the Study:

  • To investigate higher-order structure formation of peripheral membrane proteins.
  • To elucidate the role of membrane-mediated interactions in protein assembly.

Main Methods:

  • Coarse-grained membrane simulations.
  • Quantification of protein clustering using potential of mean force.

Main Results:

  • Peripheral proteins induce bilayer perturbations, facilitating assembly within and across leaflets.
  • Lipid-protein domains form on heterogeneous membranes.

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Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
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Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

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In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers
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In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers

Published on: July 28, 2018

Related Experiment Videos

Last Updated: May 31, 2026

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

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers
08:10

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers

Published on: July 28, 2018

  • Protein clustering increases with radius and hydrophobic penetration depth.

    • Conclusions:

    • Membrane-mediated interactions drive peripheral protein assembly.
    • Protein clusters may serve as templates for signaling cascades and transport intermediates.