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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...
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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.
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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 with the analogy of...
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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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A key characteristic of life is the ability to separate the external environment from the internal space. To do this, cells have evolved semi-permeable membranes that regulate the passage of biological molecules. Additionally, the cell membrane defines a cell’s shape and interactions with the external environment. Eukaryotic cell membranes also serve to compartmentalize the internal space into organelles, including the endomembrane structures of the nucleus, endoplasmic reticulum and Golgi...

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Patterning Bioactive Proteins or Peptides on Hydrogel Using Photochemistry for Biological Applications
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Patterning Bioactive Proteins or Peptides on Hydrogel Using Photochemistry for Biological Applications

Published on: September 15, 2017

Biomolecule surface patterning may enhance membrane association.

Sergey Pogodin1, Nigel K H Slater, Vladimir A Baulin

  • 1Departament d'Enginyeria Quimica, Universitat Rovira i Virgili, 26 Av. dels Paisos Catalans, 43007 Tarragona, Spain.

ACS Nano
|January 14, 2012
PubMed
Summary
This summary is machine-generated.

Amphipathic proteins spontaneously form alpha-helical structures near membranes. Their stripe patterns and membrane interactions are modeled, revealing how stripe thickness influences protein association with lipid bilayers.

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Area of Science:

  • Biophysics
  • Protein Folding
  • Membrane Biophysics

Background:

  • Amphipathic late embryogenesis abundant (LEA) proteins undergo a conformational transition from random coils to alpha-helical structures under dehydration.
  • Membrane presence promotes this alpha-helical folding transition in LEA proteins.

Purpose of the Study:

  • To investigate the thermodynamics of membrane association for alpha-helical LEA proteins.
  • To model the interaction free energy between patterned alpha-helices and phospholipid bilayers.

Main Methods:

  • Modeled alpha-helical structures as infinite rigid cylinders with axial hydrophobic and hydrophilic stripes.
  • Employed statistical thermodynamic calculations using single-chain mean-field theory.

Main Results:

  • The relative thickness of hydrophobic/hydrophilic stripes on the alpha-helices significantly controls the free energy of interaction with phospholipid bilayers.
  • Bilayer structure and the depth of cylinder penetration into the bilayer also influence the interaction free energy.
  • Identified key parameters governing the association of these proteins with membranes.

Conclusions:

  • The study provides insights into the thermodynamic principles governing LEA protein-membrane interactions.
  • Results suggest optimal stripe thickness for mimicking protein association with biological membranes.
  • This modeling approach can inform the design of proteins with specific membrane-binding properties.