ArticleJournal of biomolecular NMR2012
New amino acid residue type identification experiments valid for protonated and deuterated proteins.
Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Long-chain fatty acids block allergic reaction against lipid transfer protein Sola l 7 from tomato seeds.Protein science : a publication of the Protein Society · 2024Article
- Amino acid recognition for automatic resonance assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2016Article
- High-dimensionality 13C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2013Article
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2 authors.
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Abstract
Two experiments are presented that yield amino acid type identification of individual residues in a protein by editing the (1)H-(15)N correlations into four different 2D subspectra, each corresponding to a different amino acid type class, and that can be applied to deuterated proteins. One experiment provides information on the amino acid type of the residue preceding the detected amide (1)H-(15)N correlation, while the other gives information on the type of its own residue. Versions for protonated proteins are also presented, and in this case it is possible to classify the residues into six different classes. Both sequential and intraresidue experiments provide highly complementary information, greatly facilitating the assignment of protein resonances. The experiments will also assist in transferring the assignment of a protein to the spectra obtained under different experimental conditions (e.g. temperature, pH, presence of ligands, cofactors, etc.).
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