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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.
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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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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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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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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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Author Spotlight: Advancing Cell Membrane Biophysics - Exploring Interactions and Challenges Through Experimental and Computational Approaches
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Encapsulated membrane proteins: A simplified system for molecular simulation.

Sarah C Lee1, Syma Khalid2, Naomi L Pollock1

  • 1School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.

Biochimica Et Biophysica Acta
|March 7, 2016
PubMed
Summary
This summary is machine-generated.

New methods using nanoscale discs preserve membrane protein-lipid interactions, aiding high-resolution structure determination and simplifying complex molecular simulations for membrane proteins.

Keywords:
AmphipolsDetergent-freeLipid bilayerMembrane proteins (MP)Membrane scaffold proteins (MSP)NanodiscsStyrene maleic acid lipid particles (SMALPs)

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Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Chemistry

Background:

  • Significant advancements in atomic-level biomolecular interaction understanding have driven progress in large-scale molecular simulations.
  • Challenges persist in studying membrane proteins due to a lack of atomic resolution structures and inherent system complexity.

Purpose of the Study:

  • To review novel approaches for studying membrane proteins, focusing on methods that maintain native protein-lipid interactions.
  • To highlight techniques enabling high-resolution structure determination and simplified simulations of membrane protein systems.

Main Methods:

  • Analysis of new practical approaches for membrane protein studies.
  • Focus on methods that create nanoscale discoidal particles encapsulating membrane proteins within lipid bilayers.
  • Comparison of the Membrane Scaffold Protein (MSP) system and Styrene Maleic Acid (SMA) copolymer Lipid Particles (SMALPs).

Main Results:

  • These methods preserve essential protein-lipid interactions crucial for structure and function.
  • Nanoscale discs facilitate enhanced protein production, accelerating structure determination.
  • SMALPs and MSP systems offer simplified formats for membrane protein dynamics simulations.

Conclusions:

  • Novel nanoscale disc-based methods represent a significant advancement in membrane protein research.
  • These approaches have the potential to accelerate atomic resolution structure determination and improve the efficiency of molecular dynamics simulations.
  • Preserving the native membrane environment is key to understanding membrane protein structure and function.