{
  "abstract": "19F NMR is becoming an increasingly powerful method for studying the conformation and ligand binding of proteins in the solid state and in solution. In liquids NMR, surprisingly, reports on through‐space 19F–19F coupling remain scarce. Here, we present the first 19F–19F NOESY study designed to calibrate inter‐fluorine distances in proteins. Three difluorinated tryptophan analogues (4,5‐F2‐Trp, 4,6‐F2‐Trp, 5,6‐F2‐Trp) were synthesized and site‐specifically incorporated into human cyclophilin A (CypA). Series of 19F–19F NOESY build‐up experiments were recorded for each labeled protein, and the extracted cross‐relaxation rates were compared to fixed reference distances. While small distances in the 2.5–3.0 Å range were easily accessible, the upper limit at 14.1 T is ∼5 Å. These results provide evidence that short distances can be extracted from 19F–19F NOESY spectra, expanding the toolbox for studying protein‐protein or protein‐ligand interactions by NMR.",
  "abstract_shown": true,
  "affiliations": [
    "Department of Organic Chemistry I, Faculty of Chemistry University of the Basque Country (EHU) Donostia/San Sebastián Spain",
    "Department of Structural Biology University of Pittsburgh School of Medicine Pittsburgh Pennsylvania USA"
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 7,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Iker Hernández"
    },
    {
      "affs": [
        1
      ],
      "name": "In‐Ja L. Byeon"
    },
    {
      "affs": [
        1
      ],
      "name": "Christina M. Monnie"
    },
    {
      "affs": [
        0
      ],
      "name": "Vadim A. Soloshonok"
    },
    {
      "affs": [
        0
      ],
      "name": "Aitor Landa"
    },
    {
      "affs": [
        0
      ],
      "name": "Mikel Oiarbide"
    },
    {
      "affs": [
        1
      ],
      "name": "Angela M. Gronenborn",
      "orcid": "0000-0001-9072-3525"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/4m0xq7b8em71h.bib",
  "cited_by": 0,
  "doi": "10.1002/chem.71456",
  "fulltext_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC13715999/",
  "id": "4m0xq7b8em71h",
  "issns": [
    "0947-6539",
    "1521-3765"
  ],
  "landing_url": "https://doi.org/10.1002/chem.71456",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "heading",
      "Research Article"
    ],
    [
      "openalex",
      "1607|Advanced NMR Techniques and Applications"
    ]
  ],
  "openalex": "W7170401640",
  "pdf_url": null,
  "pmcid": "PMC13715999",
  "pmid": "42497074",
  "published": "2026-07-24",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/4m0xq7b8em71h.ris",
  "sources": [
    {
      "first_seen": "2026-11-01T12:23:09Z",
      "native_id": "PMC13715999",
      "source": "pmc",
      "url": "https://doi.org/10.1002/chem.71456"
    }
  ],
  "subjects": [
    {
      "field": "chemistry",
      "origin": "openalex:1607|Advanced NMR Techniques and Applications",
      "subfield": "physical"
    }
  ],
  "title": "Assessment of Attainable Distances in Proteins by Through‐Space 19F–19F Couplings",
  "title_text": "Assessment of Attainable Distances in Proteins by Through‐Space 19F–19F Couplings",
  "type": "peer-reviewed",
  "updated_at": "2026-11-01T12:23:09Z",
  "url": "https://research.draconitic.com/paper/4m0xq7b8em71h",
  "venue": "Chemistry (Weinheim an Der Bergstrasse, Germany)",
  "versions": []
}