Related Experiment Video
Updated: Nov 7, 2025

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
Published on: March 5, 2017
Structural biology of endogenous membrane protein assemblies in native nanodiscs
Chanelle J Brown1, Catharine Trieber2, Michael Overduin2
1Department of Chemistry and Macromolecules Innovation Institute, Virginia Tech, Blacksburg, USA.
Abstract:
The advent of amphiphilic copolymers enables integral membrane proteins to be solubilized into stable 10-30 nm native nanodiscs to resolve their multisubunit structures, post-translational modifications, endogenous lipid bilayers, and small molecule ligands. This breakthrough has positioned biological membrane:protein assemblies (memteins) as fundamental functional units of cellular membranes. Herein, we review copolymer design strategies and methods for the characterization of transmembrane proteins within native nanodiscs by cryo-electron microscopy (cryo-EM), transmission electron microscopy, nuclear magnetic resonance spectroscopy, electron paramagnetic resonance, X-ray diffraction, surface plasmon resonance, and mass spectrometry.
Related Concept Videos
Mechanisms of Membrane Domain Formation
Another mechanism for membrane domain formation involves membrane proteins interacting with...
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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...
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Tail-anchoring of Proteins in the ER Membrane
Pinching-off of Coated Vesicles

