ArticleJournal of the American Chemical Society2009
NMR resonance assignments of sparsely labeled proteins: amide proton exchange correlations in native and denatured states.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- A comprehensive assessment of selective amino acidJournal of biomolecular NMR · 2024Article
- Structural and functional characterization of Aedes aegypti pupal cuticle protein that controls dengue virus infection.Protein science : a publication of the Protein Society · 2023Article
- Design of self-assembled glycopolymeric zwitterionic micelles as removable protein stabilizing agents.Nanoscale advances · 2023Article
- AssignSLP_GUI, a software tool exploiting AI for NMR resonance assignment of sparsely labeled proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- Structural Characterization of a Heparan Sulfate Pentamer Interacting with LAR-Ig1-2.Biochemistry · 2018Article
- NMR assignments of sparsely labeled proteins using a genetic algorithm.Journal of biomolecular NMR · 2017Article
- Chemical shift prediction for denatured proteins.Journal of biomolecular NMR · 2013Article
- Multi-dimensional NMR without coherence transfer: minimizing losses in large systems.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2011Article
- Nuclear magnetic resonance structural characterization of substrates bound to the alpha-2,6-sialyltransferase, ST6Gal-I.Biochemistry · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Protein NMR assignments of large proteins using traditional triple resonance techniques depends on double or triple labeling of samples with (15)N, (13)C, and (2)H. This is not always practical with proteins that require expression in nonbacterial hosts. Labeling with isotopically labeled versions of single amino acids (sparse labeling) often is possible; however, resonance assignment then requires a new strategy. Here a procedure for the assignment of cross-peaks in (15)N-(1)H correlation spectra of sparsely labeled proteins is presented. It relies on the correlation of proton-deuterium amide exchange rates in native and denatured spectra of the intact protein, followed by correlation of chemical shifts in the spectra of the denatured protein with chemical shifts of sequenced peptides derived from the protein. The procedure is successfully demonstrated on a sample of a protein, Galectin-3, selectively labeled with (15)N at all alanine residues.
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