ArticleJournal of biomolecular NMR2011
A simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteins.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Structural basis of apoptosis induction by the mitochondrial voltage-dependent anion channel.Nature communications · 2025Article
- Structural basis of metabolite transport by the chloroplast outer envelope channel OEP21.Nature structural & molecular biology · 2023Article
- Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.Nature protocols · 2018Article
- Nuclear overhauser spectroscopy of chiral CHD methylene groups.Journal of biomolecular NMR · 2016Article
- CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample.Journal of biomolecular NMR · 2015Article
- Structure refinement and membrane positioning of selectively labeled OmpX in phospholipid nanodiscs.Journal of biomolecular NMR · 2015Article
- Protein-ligand structure guided by backbone and side-chain proton chemical shift perturbations.Journal of biomolecular NMR · 2014Article
- Stereospecific assignments in proteins using exact NOEs.Journal of biomolecular NMR · 2013Article
- Biosynthetically directed ²H labelling for stereospecific resonance assignments of glycine methylene groups.Journal of biomolecular NMR · 2013Article
- FLAMEnGO: a fuzzy logic approach for methyl group assignment using NOESY and paramagnetic relaxation enhancement data.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new method for stereospecific assignment of prochiral methyl groups in proteins is presented in which protein samples are produced using U-[(13)C]glucose and subsaturating amounts of 2-[(13)C]methyl-acetolactate. The resulting non-uniform labeling pattern allows proR and proS methyl groups to be easily distinguished by their different phases in a constant-time two-dimensional (1)H-(13)C correlation spectra. Protein samples are conveniently prepared using the same media composition as the main uniformly-labeled sample and contain higher levels of isotope-enrichment than fractional labeling approaches. This new strategy thus represents an economically-attractive, robust alternative for obtaining isotopically-encoded stereospecific NMR assignments of prochiral methyl groups.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.