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Related Concept Videos

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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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.
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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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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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Fluid Mosaic Model01:19

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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...
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Multi-pass Transmembrane Proteins and β-barrels01:09

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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 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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Related Experiment Video

Updated: May 4, 2026

Neutron Spin Echo Spectroscopy as a Unique Probe for Lipid Membrane Dynamics and Membrane-Protein Interactions
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Functional dynamics of cell surface membrane proteins.

Noritaka Nishida1, Masanori Osawa1, Koh Takeuchi2

  • 1Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|December 17, 2013
PubMed
Summary
This summary is machine-generated.

Cell surface receptors are dynamic proteins that fluctuate between conformations. NMR studies reveal these dynamics are crucial for proper receptor function, challenging traditional views of activation.

Keywords:
Cell surface receptorsDynamicsMembrane proteinsNMR

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Cell surface receptors are integral membrane proteins transmitting external stimuli across plasma membranes.
  • Conventional models depict receptor activation as a single conformational change upon ligand binding.
  • Emerging evidence suggests greater structural dynamics in these proteins.

Purpose of the Study:

  • To review NMR studies investigating the structural dynamics of cell surface membrane proteins.
  • To highlight the direct linkage between protein dynamics and function.
  • To explore the implications for understanding receptor activation.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to probe protein structure and dynamics.
  • Biochemical experiments to assess protein function.
  • Cell biological experiments to validate findings in a cellular context.

Main Results:

  • NMR studies reveal cell surface membrane proteins are highly dynamic, existing in multiple conformations.
  • These dynamical properties are not mere byproducts but are critical for proper receptor function.
  • Direct correlations between specific structural dynamics and functional states were identified.

Conclusions:

  • The dynamic nature of cell surface receptors is fundamental to their function.
  • NMR spectroscopy provides critical insights into the structure-dynamics-function relationship.
  • This review emphasizes a paradigm shift in understanding receptor activation beyond static conformational changes.