ArticleJournal of biomolecular NMR2018
Perspective: next generation isotope-aided methods for protein NMR spectroscopy.
Article in Journal of biomolecular NMR, 2018. 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, 19 citations in OpenAlex.
- NMR in the Age of Modern Biomedical Research and Drug Discovery.Journal of molecular biology · 2025Review
- Leveraging relaxation-optimizedNature chemistry · 2025Article
- Changes in the hydrophobic network of the FliGiScience · 2023Article
- Site-Specific Isotope Labeling of FliG for Studying Structural Dynamics Using Nuclear Magnetic Resonance Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Sparse isotope labeling for nuclear magnetic resonance (NMR) of glycoproteins using 13C-glucose.Glycobiology · 2021Article
- Modular control of l-tryptophan isotopic substitution via an efficient biosynthetic cascade.Organic & biomolecular chemistry · 2020Article
- Protein Structure Determination in Living Cells.International journal of molecular sciences · 2019Review
- Advanced isotopic labeling for the NMR investigation of challenging proteins and nucleic acids.Journal of biomolecular NMR · 2018Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
In this perspective, we describe our efforts to innovate the current isotope-aided NMR methodology to investigate biologically important large proteins and protein complexes, for which only limited structural information could be obtained by conventional NMR approaches. At the present time, it is widely believed that only backbone amide and methyl signals are amenable for investigating such difficult targets. Therefore, our primary mission is to disseminate our novel knowledge within the biological NMR community; specifically, that any type of NMR signals other than methyl and amide groups can be obtained, even for quite large proteins, by optimizing the transverse relaxation properties by isotope labeling methods. The idea of "TROSY by isotope labeling" has been cultivated through our endeavors aiming to improve the original stereo-array isotope labeling (SAIL) method (Kainosho et al., Nature 440:52-57, 2006). The SAIL TROSY methods subsequently culminated in the successful observations of individual NMR signals for the side-chain aliphatic and aromatic
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Registered trials
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