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Related Concept Videos

Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

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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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Protein Diffusion in the Membrane01:24

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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...
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Membrane Proteins01:30

Membrane Proteins

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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...
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Membrane Fluidity01:26

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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
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Membrane Fluidity01:23

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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.
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Introduction to Membrane Proteins01:16

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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...
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Evaluating membrane affinity by integrating protein orientations.

Fangqiang Zhu1, Matthias Clauss2

  • 1Department of Physics, Indiana University - Purdue University Indianapolis, United States.

Journal of Molecular Graphics & Modelling
|December 3, 2014
PubMed
Summary
This summary is machine-generated.

The study evaluates protein-lipid bilayer interactions, finding Epidermal Growth Factor-like Module Containing, Adipocyte-Differentiated, and Endothelial Cell-Derived Protein II (EMAPII) behaves like a water-soluble protein. Its release from cells likely involves complex mechanisms beyond passive diffusion.

Keywords:
Coarse-grained modelingEMAPIIFGF1Free energyNon-classical releaseProtein orientation

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Area of Science:

  • Biophysics
  • Computational Biology
  • Molecular Interactions

Background:

  • Protein interactions with lipid bilayers are crucial for membrane localization.
  • Epidermal Growth Factor-like Module Containing, Adipocyte-Differentiated, and Endothelial Cell-Derived Protein II (EMAPII) is released from cells via unknown mechanisms.

Purpose of the Study:

  • To evaluate the membrane interactions of EMAPII and other proteins using a computational approach.
  • To determine the free energy profiles of proteins interacting with lipid bilayers.

Main Methods:

  • A knowledge-based coarse-grained membrane potential was employed.
  • Free energy profiles were calculated by integrating out orientation degrees of freedom.
  • Protein orientation space was reduced to two dimensions on a unit sphere for computational efficiency.

Main Results:

  • Integrated free energy profiles revealed distinct characteristics for membrane and water-soluble proteins.
  • EMAPII exhibited high energetic barriers for membrane entry and crossing, typical of water-soluble proteins.
  • The findings suggest EMAPII release involves complex mechanisms, not simple passive diffusion.

Conclusions:

  • EMAPII's membrane interaction profile is consistent with a water-soluble protein.
  • The non-classical release of EMAPII from cells requires further investigation into sophisticated export pathways.