Protein Nanodisc Complex
Protein Nanodisc Complex - Related Videos
04:46
Synthesis of Nanodisc-Stabilized Membrane Protein Antigens Using a Cell-Free System
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2025
Source: Gilmore, S. F., et al. Cell-Free Scaled Production and Adjuvant Addition to a Recombinant Major Outer Membrane Protein from Chlamydia muridarum for Vaccine Development. J. Vis. Exp. (2022)This video demonstrates the cell-free synthesis of nanodisc-stabilized membrane protein antigens using a dual-compartment system. The device maintains optimal conditions for efficient protein synthesis, proper folding, and stable integration into nanodiscs.
10:21
A Technique for Stabilizing Membrane Proteins in Nanodiscs
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2026
This study outlines the procedure for reconstituting the membrane protein TWIK-related acid-sensitive K+ channel 2 (Task2) into nanodiscs. The successful assembly was confirmed by single-particle cryo-electron microscopy, which yielded well-defined two-dimensional class averages.
08:24
Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs
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Cited by 5 •
2020
Co-translational insertion into pre-formed nanodiscs makes it possible to study cell-free synthesized membrane proteins in defined lipid environments without contact with detergents. This protocol describes the preparation of essential system components and the critical parameters for improving expression efficiency and sample quality.
02:41
Protein Complex Assembly
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2020
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes. Many viruses self-assemble into a fully functional unit using the infected host cell to...
01:57
Protein Complexes with Interchangeable Parts
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2020
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct. The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
FAQs
Scaffold proteins stabilize the assembly by encircling the lipid patch after detergent is removed. Their amphipathic character allows them to associate with the membrane-facing region while shielding exposed hydrophobic edges from water. This stabilization produces a soluble, defined particle rather than leaving the membrane protein in a detergent-solubilized mixture, supporting controlled biochemical and biophysical measurements.
Lipid composition provides a way to examine how the surrounding membrane influences a protein. In a nanodisc, the target remains associated with a small lipid bilayer while researchers vary the membrane context in a defined format. Measurements can then relate composition to protein conformation, activity, or interactions, rather than treating the protein in isolation.
Detergent removal drives the transition from a solubilized mixture toward an organized membrane assembly. As detergent is removed, amphipathic scaffold proteins surround the lipid patch and protect its hydrophobic edges from water. This step is therefore central to creating a stable, soluble complex in which the membrane protein remains associated with a bilayer.
Preparation starts by combining detergent-solubilized lipids with the target membrane protein and amphipathic membrane scaffold proteins. Researchers then remove the detergent, allowing the scaffolds to encircle the lipid patch and stabilize the assembly. The resulting soluble complex can be used for downstream biochemical assays, spectroscopy, structural analysis, or interaction studies.
The format is suited to membrane proteins whose behavior depends on a surrounding lipid environment, including receptors, channels, and transporters. Embedding these targets in a defined bilayer supports investigations of their conformation, activity, and molecular interactions. This makes the approach relevant when researchers need information about membrane-associated function rather than protein behavior alone.
Protein nanodisc complexes support several complementary forms of analysis, including biochemical assays, spectroscopy, structural analysis, and interaction studies. Together, these approaches can reveal how membrane composition relates to protein conformation and activity. The defined, soluble format also allows researchers to examine membrane proteins under a controlled context while preserving a near-native lipid environment.