
Open access
Date
2021-01-14Type
- Journal Article
Citations
Cited 20 times in
Web of Science
Cited 20 times in
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ETH Bibliography
yes
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Abstract
Integral membrane proteins (IMPs) are biologically highly significant but challenging to study because they require maintaining a cellular lipid-like environment. Here, we explore the application of mass photometry (MP) to IMPs and membrane-mimetic systems at the single-particle level. We apply MP to amphipathic vehicles, such as detergents and amphipols, as well as to lipid and native nanodiscs, characterizing the particle size, sample purity, and heterogeneity. Using methods established for cryogenic electron microscopy, we eliminate detergent background, enabling high-resolution studies of membrane-protein structure and interactions. We find evidence that, when extracted from native membranes using native styrene-maleic acid nanodiscs, the potassium channel KcsA is present as a dimer of tetramers—in contrast to results obtained using detergent purification. Finally, using lipid nanodiscs, we show that MP can help distinguish between functional and non-functional nanodisc assemblies, as well as determine the critical factors for lipid nanodisc formation. © 2020 Elsevier Inc. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000455794Publication status
publishedExternal links
Journal / series
ChemVolume
Pages / Article No.
Publisher
Cell PressSubject
Mass photometry; Membrane proteins; Nanodisc; Detergent micelle; Amphipol; Single-molecule; Label-freeOrganisational unit
03782 - Riek, Roland / Riek, Roland
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Show all metadata
Citations
Cited 20 times in
Web of Science
Cited 20 times in
Scopus
ETH Bibliography
yes
Altmetrics