ArticleJournal of biomolecular NMR2013
Biosynthetically directed ²H labelling for stereospecific resonance assignments of glycine methylene groups.
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 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Side-chain-selective deuterium labeling by a simple bio-expression method enhances resolution and simplifies spectra inJournal of biomolecular NMR · 2025Article
- Alpha protons as NMR probes in deuterated proteins.Journal of biomolecular NMR · 2019Article
- Selective (15)N-labeling of the side-chain amide groups of asparagine and glutamine for applications in paramagnetic NMR spectroscopy.Journal of biomolecular NMR · 2014Article
- Advances in NMR structures of integral membrane proteins.Current opinion in structural biology · 2013Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Stereospecific resonance assignments of the α-protons of glycine are often difficult to obtain by measurements of scalar coupling constants or nuclear Overhauser effects. Here we show that these stereospecific resonance assignments can readily be obtained by cell-free protein synthesis in D(2)O, as the serine hydroxymethyltransferase, that is naturally present in E. coli cell extracts, selectively replaces the pro-2S proton of glycine by a deuterium. To encourage the conversion by serine hydroxymethyltransferase, we performed the cell-free reaction without the addition of any glycine, exploiting the capability of the enzyme to convert serine to glycine with the help of tetrahydrofolate. (13)C-HSQC spectra of ubiquitin produced with (13)C/(15)N-serine showed that about a quarter of the glycine residues derived from serine were stereospecifically deuterated. Pulse sequences are presented that select the signals from the stereospecifically deuterated glycine residues.
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