ArticleJournal of the American Chemical Society2012
Structure determination of a membrane protein in proteoliposomes.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 82 citations in OpenAlex.
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- Nanodisc reconstitution and characterization of amyloid-β precursor protein C99.bioRxiv : the preprint server for biology · 2024Article
- Solid-State NMR of Membrane Proteins in Lipid Bilayers: To Spin or Not To Spin?Accounts of chemical research · 2021Review
- Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021Article
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- Membrane proteins in magnetically aligned phospholipid polymer discs for solid-state NMR spectroscopy.Biochimica et biophysica acta. Biomembranes · 2020Article
- A Minimal Membrane Metal Transport System: Dynamics and Energetics of mer Proteins.Journal of computational chemistry · 2020Article
- A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.Australian journal of chemistry · 2020Article
- Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic TBiophysical journal · 2018Article
- Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes.Scientific reports · 2017Article
- High resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes.Journal of biomolecular NMR · 2017Article
- Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs.Angewandte Chemie (International ed. in English) · 2017Article
- Cloning, Expression, Isotope Labeling, and Purification of Transmembrane Protein MerF from Mercury ResistantFrontiers in microbiology · 2017Article
- NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.Biophysical journal · 2016Article
- Structure determination of uniformly (13)C, (15)N labeled protein using qualitative distance restraints from MAS solid-state (13)C-NMR observed paramagnetic relaxation enhancement.Journal of biomolecular NMR · 2016Article
- Spatial reorientation experiments for NMR of solids and partially oriented liquids.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015Review
- Efficient cellular solid-state NMR of membrane proteins by targeted protein labeling.Journal of biomolecular NMR · 2015Article
- Solid-state NMR and membrane proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
An NMR method for determining the three-dimensional structures of membrane proteins in proteoliposomes is demonstrated by determining the structure of MerFt, the 60-residue helix-loop-helix integral membrane core of the 81-residue mercury transporter MerF. The method merges elements of oriented sample (OS) solid-state NMR and magic angle spinning (MAS) solid-state NMR techniques to measure orientation restraints relative to a single external axis (the bilayer normal) from individual residues in a uniformly (13)C/(15)N labeled protein in unoriented liquid crystalline phospholipid bilayers. The method relies on the fast (>10(5) Hz) rotational diffusion of membrane proteins in bilayers to average the static chemical shift anisotropy and heteronuclear dipole-dipole coupling powder patterns to axially symmetric powder patterns with reduced frequency spans. The frequency associated with the parallel edge of such motionally averaged powder patterns is exactly the same as that measured from the single line resonance in the spectrum of a stationary sample that is macroscopically aligned parallel to the direction of the applied magnetic field. All data are collected on unoriented samples undergoing MAS. Averaging of the homonuclear (13)C/(13)C dipolar couplings, by MAS of the sample, enables the use of uniformly (13)C/(15)N labeled proteins, which provides enhanced sensitivity through direct (13)C detection as well as the use of multidimensional MAS solid-state NMR methods for resolving and assigning resonances. The unique feature of this method is the measurement of orientation restraints that enable the protein structure and orientation to be determined in unoriented proteoliposomes.
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