ArticleBiochimica et biophysica acta. Biomembranes2020
Membrane proteins in magnetically aligned phospholipid polymer discs for solid-state NMR spectroscopy.
Article in Biochimica et biophysica acta. Biomembranes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Peptoid-based macrodiscs of variable lipid composition for structural studies of membrane proteins by oriented-sample solid-state NMR.Journal of structural biology: X · 2024Article
- Characterization of nanodisc-forming peptides for membrane protein studies.Journal of colloid and interface science · 2024Article
- Polymer-Nanodiscs as a Novel Alignment Medium for High-Resolution NMR-Based Structural Studies of Nucleic Acids.Biomolecules · 2022Article
- Aligned peptoid-based macrodiscs for structural studies of membrane proteins by oriented-sample NMR.Biophysical journal · 2022Article
- Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.Biomolecules · 2022Review
- Dielectric dispersion characteristics of the phospholipid bilayer with subnanometer resolution from terahertz to mid-infrared.Frontiers in bioengineering and biotechnology · 2022Article
- Article
- Biological insights from SMA-extracted proteins.Biochemical Society transactions · 2021Review
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- Structure and Dynamics of GPCRs in Lipid Membranes: Physical Principles and Experimental Approaches.Molecules (Basel, Switzerland) · 2020Review
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7 authors.
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Abstract
Well-hydrated phospholipid bilayers provide a near-native environment for membrane proteins. They enable the preparation of chemically-defined samples suitable for NMR and other spectroscopic experiments that reveal the structure, dynamics, and functional interactions of the proteins at atomic resolution. The synthetic polymer styrene maleic acid (SMA) can be used to prepare detergent-free samples that form macrodiscs with diameters greater than 30 nm at room temperature, and spontaneously align in the magnetic field of an NMR spectrometer at temperatures above 35 °C. Here we show that magnetically aligned macrodiscs are particularly well suited for solid-state NMR experiments of membrane proteins because the SMA-lipid assembly both immobilizes the embedded protein and provides uniaxial order for oriented sample (OS) solid-state NMR studies. We show that aligned macrodiscs incorporating four different membrane proteins with a wide range of sizes and topological complexity yield high-resolution OS solid-state NMR spectra. The work is dedicated to Michelle Auger who made key contributions to the field of membrane and membrane protein biophysics.
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