ArticleBiophysical journal2006
Structural analysis of nanoscale self-assembled discoidal lipid bilayers by solid-state NMR spectroscopy.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
35 citing papers in PubMed, 89 citations in OpenAlex.
- Toward Nanodisc Tailoring for SANS Study of Membrane Proteins.Bioengineering (Basel, Switzerland) · 2026Article
- Electron videography of a lipid-protein tango.Science advances · 2024Article
- Effects of Amylopectins from Five Different Sources on Disulfide Bond Formation in Alkali-Soluble Glutenin.Foods (Basel, Switzerland) · 2023Article
- A comparative study of interfacial environments in lipid nanodiscs and vesicles.Biophysical reports · 2022Article
- Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021Review
- Confinement in Nanodiscs Anisotropically Modifies Lipid Bilayer Elastic Properties.The journal of physical chemistry. B · 2020Article
- The hydrodynamic motion of Nanodiscs.Chemistry and physics of lipids · 2019Article
- Supramolecular Organization of Apolipoprotein-A-I-Derived Peptides within Disc-like Arrangements.Biophysical journal · 2018Article
- Nanodiscs: A Controlled Bilayer Surface for the Study of Membrane Proteins.Annual review of biophysics · 2018Article
- Lipid environment of membrane proteins in cryo-EM based structural analysis.Biophysical reviews · 2018Review
- Lipid Internal Dynamics Probed in Nanodiscs.Chemphyschem : a European journal of chemical physics and physical chemistry · 2017Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Nanodiscs for structural and functional studies of membrane proteins.Nature structural & molecular biology · 2016Review
- Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.Journal of biomolecular NMR · 2015Article
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- ABCA1 dimer-monomer interconversion during HDL generation revealed by single-molecule imaging.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Nanodiscs as a new tool to examine lipid-protein interactions.Methods in molecular biology (Clifton, N.J.) · 2013Review
- Nanodiscs versus macrodiscs for NMR of membrane proteins.Biochemistry · 2011Review
- Conformational transitions in the membrane scaffold protein of phospholipid bilayer nanodiscs.Molecular & cellular proteomics : MCP · 2011Article
- Nanoscale studies of protein-membrane interactions in blood clotting.Journal of thrombosis and haemostasis : JTH · 2011Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Nanodiscs are an example of discoidal nanoscale self-assembled lipid/protein particles similar to nascent high-density lipoproteins, which reduce the risk of coronary artery disease. The major protein component of high-density lipoproteins is human apolipoprotein A-I, and the corresponding protein component of Nanodiscs is membrane scaffold protein 1 (MSP1), a 200-residue lipid-binding domain of human apolipoprotein A-I. Here we present magic-angle spinning (MAS) solid-state NMR studies of uniformly (13)C,(15)N-labeled MSP1 in polyethylene glycol precipitated Nanodiscs. Two-dimensional MAS (13)C-(13)C correlation spectra show excellent microscopic order of MSP1 in precipitated Nanodiscs. Secondary isotropic chemical shifts throughout the protein are consistent with a predominantly helical structure. Moreover, the backbone conformations of prolines derived from their (13)C chemical shifts are consistent with the molecular belt model but not the picket fence model of lipid-bound MSP1. Overall comparison of experimental spectra and (13)C chemical shifts predicted from several structural models also favors the belt model. Our study thus supports the belt model of Nanodisc structure and demonstrates the utility of MAS NMR to study the structure of high molecular weight lipid-protein complexes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.