ArticleNature communications2018
Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment.
Article in Nature communications, 2018. 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.
- Facilitating NMR Resonance Assignment with Metabolic Tampering.bioRxiv : the preprint server for biology · 2026Article
- NMR in the Age of Modern Biomedical Research and Drug Discovery.Journal of molecular biology · 2025Review
- Exploring the biochemical landscape of bacterial medium with pyruvate as the exclusive carbon source for NMR studies.Journal of biomolecular NMR · 2025Article
- Protein NMR assignment by isotope pattern recognition.Science advances · 2024Article
- Bacterial Transcriptional Regulators: A Road Map for Functional, Structural, and Biophysical Characterization.International journal of molecular sciences · 2022Review
- EvolvingInternational journal of molecular sciences · 2021Article
- Enhancing Compression Level for More Efficient Compressed Sensing and Other Lessons from NMR Spectroscopy.Sensors (Basel, Switzerland) · 2020Article
- Emerging solution NMR methods to illuminate the structural and dynamic properties of proteins.Current opinion in structural biology · 2019Review
- NMR: an essential structural tool for integrative studies of T cell development, pMHC ligand recognition and TCR mechanobiology.Journal of biomolecular NMR · 2019Article
- Isotopic Labeling of Eukaryotic Membrane Proteins for NMR Studies of Interactions and Dynamics.Methods in enzymology · 2019Article
- Optimal control theory enables homonuclear decoupling without Bloch-Siegert shifts in NMR spectroscopy.Nature communications · 2018Article
- Late metabolic precursors for selective aromatic residue labeling.Journal of biomolecular NMR · 2018Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Backbone resonance assignment is a critical first step in the investigation of proteins by NMR. This is traditionally achieved with a standard set of experiments, most of which are not optimal for large proteins. Of these, HNCA is the most sensitive experiment that provides sequential correlations. However, this experiment suffers from chemical shift degeneracy problems during the assignment procedure. We present a strategy that increases the effective resolution of HNCA and enables near-complete resonance assignment using this single HNCA experiment. We utilize a combination of 2-
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