ArticleChemistry and physics of lipids2019
The hydrodynamic motion of Nanodiscs.
Article in Chemistry and physics of lipids, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Understanding charged polymer-lipid interactions in model membranes revealed by EPR and solid-state NMR: Implications for membrane protein studies.Chemistry and physics of lipids · 2026Article
- Measurement of Residual Dipolar Couplings Using Magnetically Aligned and Flipped Nanodiscs.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Solid-State NMR Study to Probe the Effects of Divalent Metal Ions (CaLangmuir : the ACS journal of surfaces and colloids · 2021Article
- Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021Review
- Dark, Ultra-Dark and Ultra-Bright Nanodiscs for membrane protein investigations.Analytical biochemistry · 2020Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
We present a fluorescence-based methodology for monitoring the rotational dynamics of Nanodiscs. Nanodiscs are nano-scale lipid bilayers surrounded by a helical membrane scaffold protein (MSP) that have found considerable use in studying the interactions between membrane proteins and their lipid bilayer environment. Using a long-lifetime Ruthenium label covalently attached to the Nanodiscs, we find that Nanodiscs of increasing diameter, made by varying the number of helical repeats in the MSP, display increasing rotational correlation times. We also model our system using both analytical equations that describe rotating spheroids and numerical calculations performed on atomic models of Nanodiscs. Using these methods, we observe a linear relationship between the experimentally determined rotational correlation times and those calculated from both analytical equations and numerical solutions. This work sets the stage for accurate, label-free quantification of protein-lipid interactions at the membrane surface.
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Registered trials
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