ArticleJournal of biomolecular NMR2025
Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding.
Article in Journal of biomolecular NMR, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Structure-activity of outer membrane proteins in native bacterial membrane vesicles by solid-state NMR.bioRxiv : the preprint server for biology · 2026Article
- In situ NMR reveals a pH sensor motif in an outer membrane protein that drives bacterial vesicle production.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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5 authors.
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Abstract
The NMR signals from protein sidechains are rich in information about intra- and inter-molecular interactions, but their detection can be complicated due to spectral overlap as well as conformational and hydrogen exchange. In this work, we demonstrate a protocol for multi-dimensional solid-state NMR spectral editing of signals from basic sidechains based on Hadamard matrix encoding. The Hadamard method acquires multi-dimensional experiments in such a way that both the backbone and under-sampled sidechain signals can be decoded for unambiguous editing in the
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