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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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Updated: Aug 26, 2025

Author Spotlight: Advancing Cell Membrane Biophysics - Exploring Interactions and Challenges Through Experimental and Computational Approaches

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mPPases create a conserved anionic membrane fingerprint as identified via multi-scale simulations.

Alexandra O M Holmes¹, Adrian Goldman^1,2, Antreas C Kalli³

¹School of Biomedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.

Plos Computational Biology

|October 3, 2022

Summary

Membrane-integral pyrophosphatases (mPPases) are crucial enzymes. New simulations reveal specific anionic lipid interactions at four sites, potentially key to mPPase function and stability.

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Published on: October 21, 2018

Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Membrane-integral pyrophosphatases (mPPases) are vital membrane-bound enzymes.
They hydrolyze inorganic pyrophosphate and translocate cations, impacting parasite infectivity and plant development.
Emerging evidence suggests the membrane environment significantly influences mPPase function.

Purpose of the Study:

To investigate the role of the membrane environment in mPPase mechanism.
To identify specific lipid interactions with mPPases using advanced simulation techniques.

Main Methods:

Multiscale molecular dynamics simulations were employed.
Simulations were performed on mPPases from Thermotoga maritima, Vigna radiata, and Clostridium leptum.

Main Results:

Specific anionic lipid interactions were identified at four distinct sites on mPPases.
These interactions occur at both distal and interfacial regions of the protein.
Conserved interactions involve positively charged residues on specific helices (1-4 for distal, 9-14 for interfacial).

Conclusions:

Anionic lipid interactions are a conserved feature of mPPases.
These interactions likely play a critical role in protein stability and function.
Findings provide a basis for future structural and functional studies of mPPases.