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Related Concept Videos

Fluid Mosaic Model01:19

Fluid Mosaic Model

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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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Mechanisms of Membrane Domain Formation00:59

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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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Membrane Domains01:18

Membrane Domains

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The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
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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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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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Single-pass Transmembrane Proteins01:25

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

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Atomic-level analysis of membrane-protein structure.

Wayne A Hendrickson1

  • 1Department of Biochemistry and Molecular Biophysics and the Department of Physiology and Cellular Biophysics, Columbia University, New York, New York, USA, and at the New York Structural Biology Center (NYSBC), New York, New York, USA.

Nature Structural & Molecular Biology
|June 9, 2016
PubMed
Summary
This summary is machine-generated.

Determining the atomic-level structures of membrane proteins, which are difficult to study, is accelerating. Advances in protein production and analysis methods are key to this progress.

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Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Membrane proteins are crucial for cellular functions but are underrepresented in structural databases due to analysis challenges.
  • Structural analysis of membrane proteins is significantly more difficult compared to soluble proteins.

Purpose of the Study:

  • To highlight recent advancements in membrane protein structure determination.
  • To underscore the impact of new methodologies on structural biology.

Main Methods:

  • Recent advances in protein production techniques.
  • Improved crystallographic analysis methods.
  • Progress in cryo-electron microscopy (cryo-EM) analysis.

Main Results:

  • Accelerated pace of atomic-level structure determination for membrane proteins.
  • Increased representation of membrane proteins in structural databases is anticipated.

Conclusions:

  • Focused consortium efforts and methodological improvements are driving progress in membrane protein structural biology.
  • Future structural studies will benefit from these advancements, enhancing our understanding of membrane protein function.