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Related Concept Videos

Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
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Microbial membranes exhibit remarkable diversity in lipid composition, reflecting evolutionary adaptations to various environmental conditions. The three domains of life—Bacteria, Archaea, and Eukarya—synthesize membrane lipids through distinct biosynthetic pathways, leading to fundamental structural differences that impact membrane stability, function, and adaptability.Fatty Acid-Based Lipids in Bacteria and EukaryaBacteria and eukaryotes share a common fatty acid biosynthesis pathway, which...
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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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Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy
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Monotopic enzymes and lipid bilayers: a comparative study.

Philip W Fowler1, Kia Balali-Mood, Sundeep Deol

  • 1Department of Biochemistry, University of Oxford, UK.

Biochemistry
|February 22, 2007
PubMed
Summary

Molecular dynamics simulations reveal how two monotopic proteins, monoamine oxidase B (MAO-B) and cyclooxygenase-2 (COX-2), interact with cell membranes. Basic residues are key to binding, forming hydrogen bonds with phospholipids and influencing lipid order.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Computational Biophysics

Background:

  • Monotopic proteins are membrane proteins that associate with but do not penetrate cell membranes.
  • Understanding their interaction with the lipid bilayer is crucial for elucidating cellular functions.

Purpose of the Study:

  • To compare the membrane binding mechanisms of two distinct monotopic proteins: monoamine oxidase B (MAO-B) and cyclooxygenase-2 (COX-2).
  • To investigate the role of specific amino acid residues and hydrogen bonding in protein-bilayer interactions.

Main Methods:

  • Utilizing molecular dynamics simulations to model the interaction of MAO-B and COX-2 with a phospholipid bilayer.
  • Analyzing lipid order parameters to assess the impact of protein binding on membrane structure.
  • Identifying key residues involved in phospholipid binding through atomistic proximity analysis.

Main Results:

  • Both MAO-B and COX-2 form hydrogen bonds with the phospholipid bilayer, primarily through basic amino acid side chains.
  • COX-2 minimally perturbs the bilayer, affecting mainly the upper leaflet.
  • MAO-B induces differential ordering of lipid tails, increasing order in the upper leaflet and decreasing it in the lower leaflet.

Conclusions:

  • The findings support existing models of monotopic protein-bilayer interactions derived from crystallographic data.
  • Basic residues play a significant role in anchoring monotopic proteins to membranes via hydrogen bonds with phospholipids.
  • The distinct effects of MAO-B and COX-2 on lipid order highlight varied mechanisms of membrane association.