ArticleJournal of the American Chemical Society2025
Assignment-Free Determination of Ligand Binding Sites in Proteins by Solid-State NMR.
Article in Journal of the American Chemical Society, 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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Who cites it
2 citing papers in PubMed.
- Conformation-selective detection of residues in solid proteins under magic-angle-spinning.Journal of biomolecular NMR · 2026Article
- Conserved Transmembrane Asparagine Is Essential for the Ion-Conducting Structure and Dynamics of the SARS-CoV-2 Envelope Protein.Journal of the American Chemical Society · 2026Article
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Authors and funding
3 authors.
Funding
Abstract
Solid-state NMR studies of ligand binding sites in proteins traditionally require assignment of the observed resonances to the amino acid sequence. This sequential assignment is time-consuming and constitutes a major bottleneck in protein solid-state NMR. To determine ligand binding sites in proteins whose structures are already known, experimentally measured protein-ligand distances can be analyzed much more rapidly if sequential assignment can be bypassed. Here we present an assignment-free NMR approach for determining ligand binding sites in proteins. We measure 2D
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Registered trials
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