ArticleJournal of biomolecular NMR2013
Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles.
Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Chiral Polyacetylene-PDMS-Copolymer-Gels as Enantiodifferentiating Alignment Media.Magnetic resonance in chemistry : MRC · 2025Article
- The architecture of transmembrane and cytoplasmic juxtamembrane regions of Toll-like receptors.Nature communications · 2023Article
- Polymer-Nanodiscs as a Novel Alignment Medium for High-Resolution NMR-Based Structural Studies of Nucleic Acids.Biomolecules · 2022Article
- Measurement of Residual Dipolar Couplings Using Magnetically Aligned and Flipped Nanodiscs.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Magnetic Alignment of Polymer Macro-Nanodiscs Enables Residual-Dipolar-Coupling-Based High-Resolution Structural Studies by NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2019Article
- Conformational dynamics and alignment properties of loop lanthanide-binding-tags (LBTs) studied in interleukin-1β.Journal of biomolecular NMR · 2017Article
- Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations.Frontiers in molecular biosciences · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
We demonstrate that alignment of a structured peptide or small protein solubilized in mixed phospholipid:detergent micelles or bicelles, when embedded in a compressed gel or liquid crystalline medium, can be altered by either changing the phospholipid aggregate shape, charge, or both together. For the hemagglutinin fusion peptide solubilized in bicelles, we show that bicelle shape and charge do not change its helical hairpin structure but impact its alignment relative to the alignment medium, both in charged compressed acrylamide gel and in liquid crystalline d(GpG). The method can be used to generate sets of residual dipolar couplings that correspond to orthogonal alignment tensors, and holds promise for high-resolution structural refinement and dynamic mapping of membrane proteins.
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Registered trials
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