ArticleJournal of biomolecular NMR2013
Selectively dispersed isotope labeling for protein structure determination by magic angle spinning NMR.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Analysis of the MODIST Sequence for Selective Proton-Proton Recoupling.The journal of physical chemistry. A · 2025Article
- Great Offset Difference Internuclear Selective Transfer.The journal of physical chemistry letters · 2023Article
- Status of Metabolomic Measurement for Insights in Alzheimer's Disease Progression-What Is Missing?International journal of molecular sciences · 2023Review
- Modest Offset Difference Internuclear Selective Transfer via Homonuclear Dipolar Coupling.The journal of physical chemistry letters · 2022Article
- Extensively sparseJournal of biomolecular NMR · 2021Article
- NMR Spectroscopy for Metabolomics Research.Metabolites · 2019Review
- Current NMR Techniques for Structure-Based Drug Discovery.Molecules (Basel, Switzerland) · 2018Review
- Proton-Assisted Recoupling (PAR) in Peptides and Proteins.The journal of physical chemistry. B · 2017Article
- Aggregation and Fibril Structure of AβBiochemistry · 2017Article
- Site-selectiveJournal of biomolecular NMR · 2017Article
- Peptide and Protein Dynamics and Low-Temperature/DNP Magic Angle Spinning NMR.The journal of physical chemistry. B · 2017Article
- Modern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life Scientists.Computational and structural biotechnology journal · 2017Review
- Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment.Journal of biomolecular NMR · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The power of nuclear magnetic resonance spectroscopy derives from its site-specific access to chemical, structural and dynamic information. However, the corresponding multiplicity of interactions can be difficult to tease apart. Complimentary approaches involve spectral editing on the one hand and selective isotope substitution on the other. Here we present a new "redox" approach to the latter: acetate is chosen as the sole carbon source for the extreme oxidation numbers of its two carbons. Consistent with conventional anabolic pathways for the amino acids, [1-(13)C] acetate does not label α carbons, labels other aliphatic carbons and the aromatic carbons very selectively, and labels the carboxyl carbons heavily. The benefits of this labeling scheme are exemplified by magic angle spinning spectra of microcrystalline immunoglobulin binding protein G (GB1): the elimination of most J-couplings and one- and two-bond dipolar couplings provides narrow signals and long-range, intra- and inter-residue, recoupling essential for distance constraints. Inverse redox labeling, from [2-(13)C] acetate, is also expected to be useful: although it retains one-bond couplings in the sidechains, the removal of CA-CO coupling in the backbone should improve the resolution of NCACX spectra.
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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.