ArticleFrontiers in molecular biosciences2022
NMR Assignment of Methyl Groups in Immobilized Proteins Using Multiple-Bond
Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Solid-state NMR spectroscopy reveals unique properties ofCell surface (Amsterdam, Netherlands) · 2025Article
- High-dimensional solid-state NMR facilitated by transverse-mixing optimal control.Research square · 2025Article
- Evaluation of TOCSY mixing for sensitivity-enhancement in solid-state NMR and application of 4D experiments for side-chain assignments of the full-length 30 kDa membrane protein GlpG.Journal of biomolecular NMR · 2025Article
- Analysis of the MODIST Sequence for Selective Proton-Proton Recoupling.The journal of physical chemistry. A · 2025Article
- Structural characterization of E22G AβPhysical chemistry chemical physics : PCCP · 2024Article
- High and fast: NMR protein-proton side-chain assignments at 160 kHz and 1.2 GHz.Chemical science · 2023Article
- Article
- Assignment of aromatic side-chain spins and characterization of their distance restraints at fast MAS.Journal of structural biology: X · 2023Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In nuclear magnetic resonance spectroscopy of proteins, methyl protons play a particular role as extremely sensitive reporters on dynamics, allosteric effects, and protein-protein interactions, accessible even in high-molecular-weight systems approaching 1 MDa. The notorious issue of their chemical shift assignment is addressed here by a joint use of solid-state
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