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Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
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%...
Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

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...
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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Related Experiment Video

Updated: Jun 12, 2026

Assembly of Cell Mimicking Supported and Suspended Lipid Bilayer Models for the Study of Molecular Interactions
12:18

Assembly of Cell Mimicking Supported and Suspended Lipid Bilayer Models for the Study of Molecular Interactions

Published on: August 3, 2021

How does proteinase 3 interact with lipid bilayers?

Torben Broemstrup1, Nathalie Reuter

  • 1Department of Informatics, University of Bergen, 5008, Bergen, Norway. torben.broemstrup@cbu.uib.no

Physical Chemistry Chemical Physics : PCCP
|June 10, 2010
PubMed
Summary
This summary is machine-generated.

Proteinase 3 (PR3), a neutrophil serine protease, anchors to cell membranes via hydrogen bonds, hydrophobic interactions, and cation-pi interactions. Its membrane proximity may affect ligand binding in inflammatory diseases.

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Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions
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Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.
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Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.

Published on: April 5, 2018

Related Experiment Videos

Last Updated: Jun 12, 2026

Assembly of Cell Mimicking Supported and Suspended Lipid Bilayer Models for the Study of Molecular Interactions
12:18

Assembly of Cell Mimicking Supported and Suspended Lipid Bilayer Models for the Study of Molecular Interactions

Published on: August 3, 2021

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions
04:45

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions

Published on: February 10, 2022

Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.
11:10

Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.

Published on: April 5, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Computational Biophysics

Background:

  • Neutrophil serine protease Proteinase 3 (PR3) is implicated in inflammatory diseases.
  • PR3 membrane expression is significant in these pathologies.
  • Previous studies show PR3 interacts with phospholipid bilayers.

Purpose of the Study:

  • To model the membrane-bound structure of PR3.
  • To elucidate the molecular interactions anchoring PR3 to phospholipid bilayers.
  • To investigate the impact of membrane binding on PR3's active site and ligand binding.

Main Methods:

  • Molecular dynamics simulations were performed.
  • PR3 was simulated anchored to dimyristoylphosphatidylcholine (DMPC), dimyristoylphosphatidylglycerol (DMPG), and DMPC/DMPG bilayers.
  • Interactions between PR3 and lipid components were analyzed.

Main Results:

  • A detailed model of membrane-bound PR3 was generated.
  • Three interaction types stabilize PR3: hydrogen bonds (basic residues with lipid headgroups), hydrophobic interactions (amino acids in bilayer core), and cation-pi interactions (aromatic residues with DMPC choline groups).
  • PR3 exhibits peripheral membrane protein characteristics, binding anionic phospholipids, with its catalytic triad unperturbed but ligand binding sites near the membrane.

Conclusions:

  • PR3 anchors to membranes through a combination of electrostatic and hydrophobic interactions.
  • The enzyme's peripheral membrane association is confirmed.
  • Membrane proximity may alter PR3's interaction with longer ligands, potentially influencing its role in inflammatory conditions.