Related Experiment Video
Updated: Jun 21, 2025

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
Published on: March 5, 2017
Elucidating the complex membrane binding of a protein with multiple anchoring domains using extHMMM
Jesper J Madsen1,2, Y Zenmei Ohkubo3
1Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, Florida, United States of America.
Coagulation factor Va (FVa) protein binding to membranes involves domain reorganization and molecular tilt. Specific residues prefer phosphatidylserine lipids, driven mainly by electrostatic interactions, revealing complex protein-membrane dynamics.
Area of Science:
- Biochemistry
- Molecular Biology
- Computational Biophysics
Background:
- Protein-membrane interactions are vital but complex.
- Coagulation factor Va (FVa) has multiple membrane-binding domains.
Purpose of the Study:
- Investigate FVa's membrane binding mechanisms.
- Identify factors governing FVa-membrane interactions.
Main Methods:
- Utilized molecular dynamics simulations.
- Employed an updated HMMM model (extHMMM).
Main Results:
- FVa adopts upright or tilted orientations.
- Domain organization deviates from crystallographic structures.
- Specific residues show lipid preference (PS over PC) via electrostatic interactions.
Conclusions:
- FVa membrane binding involves domain reorganization and tilt.
- Electrostatic interactions drive lipid preference.
- Elucidates complex protein-membrane binding dynamics.
More Related Videos
10:17Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
Published on: January 14, 2020
09:30Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
Published on: August 6, 2018
Related Concept Videos
Lipids as Anchors
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
Tail-anchoring of Proteins in the ER Membrane
GPI Anchoring of Proteins in the ER Membrane
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
Membrane Domains
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
Mechanisms of Membrane Domain Formation
Another mechanism for membrane domain formation involves membrane proteins interacting with...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...