ArticleJournal of biomolecular NMR2015
Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.
Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs.Life (Basel, Switzerland) · 2021Article
- Methods for the solubilisation of membrane proteins: the micelle-aneous world of membrane protein solubilisation.Biochemical Society transactions · 2021Review
- Calcium and hydroxyapatite binding site of human vitronectin provides insights to abnormal deposit formation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Determination of virulence associated immunogenic proteins in some ofVeterinary research forum : an international quarterly journal · 2019Article
- New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.Nature protocols · 2018Article
- Review
- Nanodiscs for structural and functional studies of membrane proteins.Nature structural & molecular biology · 2016Review
- The styrene-maleic acid copolymer: a versatile tool in membrane research.European biophysics journal : EBJ · 2016Review
- Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation.Journal of biomolecular NMR · 2015Article
- NMR studies of membrane proteins.Journal of biomolecular NMR · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Solid-state NMR studies of sedimented soluble proteins has been developed recently as an attractive approach for overcoming the size limitations of solution NMR spectroscopy while bypassing the need for sample crystallization or precipitation (Bertini et al. Proc Natl Acad Sci USA 108(26):10396-10399, 2011). Inspired by the potential benefits of this method, we have investigated the ability to sediment lipid bilayer nanodiscs reconstituted with a membrane protein. In this study, we show that nanodiscs containing the outer membrane protein Ail from Yersinia pestis can be sedimented for solid-state NMR structural studies, without the need for precipitation or lyophilization. Optimized preparations of Ail in phospholipid nanodiscs support both the structure and the fibronectin binding activity of the protein. The same sample can be used for solution NMR, solid-state NMR and activity assays, facilitating structure-activity correlation experiments across a wide range of timescales.
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