ArticleMolecular & cellular proteomics : MCP2011
Conformational transitions in the membrane scaffold protein of phospholipid bilayer nanodiscs.
Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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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
39 citing papers in PubMed.
- Electron videography of a lipid-protein tango.Science advances · 2024Article
- Molecular mechanism of muscarinic acetylcholine receptor M3 interaction with Gq.Communications biology · 2024Article
- Cooperative transitions involving hydrophobic polyelectrolytes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Chromatographic Phospholipid Trapping for Automated H/D Exchange Mass Spectrometry of Membrane Protein-Lipid Assemblies.Analytical chemistry · 2023Article
- Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutations.Nature communications · 2022Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021Review
- Nanodiscs and Mass Spectrometry: Making Membranes Fly.International journal of mass spectrometry · 2020Article
- Structural analysis of lecithin:cholesterol acyltransferase bound to high density lipoprotein particles.Communications biology · 2020Article
- Reconstitution of Membrane Proteins into Platforms Suitable for Biophysical and Structural Analyses.Methods in molecular biology (Clifton, N.J.) · 2020Article
- The hydrodynamic motion of Nanodiscs.Chemistry and physics of lipids · 2019Article
- Hydrogen-deuterium exchange mass spectrometry of membrane proteins in lipid nanodiscs.Chemistry and physics of lipids · 2019Review
- Tracking Higher Order Protein Structure by Hydrogen-Deuterium Exchange Mass Spectrometry.Protein and peptide letters · 2019Review
- Effects of Disease-Causing Mutations on the Conformation of Human Apolipoprotein A-I in Model Lipoproteins.Biochemistry · 2018Article
- Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.Nature protocols · 2018Article
- Microfluidic platform for efficient Nanodisc assembly, membrane protein incorporation, and purification.Lab on a chip · 2017Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Lipid-Mediated Regulation of Embedded Receptor Kinases via Parallel Allosteric Relays.Biophysical journal · 2017Article
- Conformational insight into multi-protein signaling assemblies by hydrogen-deuterium exchange mass spectrometry.Current opinion in structural biology · 2016Review
- Fast Photochemical Oxidation of Proteins Maps the Topology of Intrinsic Membrane Proteins: Light-Harvesting Complex 2 in a Nanodisc.Analytical chemistry · 2016Article
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6 authors.
Funding
Abstract
Phospholipid bilayer nanodiscs are model membrane systems that provide an environment where membrane proteins are highly stable and monodisperse without the use of detergents or liposomes. Nanodiscs consist of a discoidal phospholipid bilayer encircled by two copies of an amphipathic alpha helical membrane scaffold protein, which is modeled from apolipoprotein A-1. Hydrogen exchange mass spectrometry was used to probe the structure and dynamics of the scaffold protein in the presence and absence of lipid. On nanodisc self-assembly, the entire scaffold protein gained significant protection from exchange, consistent with a large, protein-wide, structural rearrangement. This protection was short-lived and the scaffold protein was highly deuterated within 2 h. Several regions of the scaffold protein, in both the lipid-free and lipid-associated states, displayed EX1 unfolding kinetics. The rapid deuteration of the scaffold protein and the presence of correlated unfolding events both indicate that nanodiscs are dynamic rather than rigid bodies in solution. This work provides a catalog of the expected scaffold protein peptic peptides in a nanodisc-hydrogen exchange mass spectrometry experiment and their deuterium uptake signatures, data that can be used as a benchmark to verify correct assembly and nanodisc structure. Such reference data will be useful control data for all hydrogen exchange mass spectrometry experiments involving nanodiscs in which transmembrane or lipid-associated proteins are the primary molecule(s) of interest.
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