{
  "abstract": "Specific isotopic labelling of proteins has greatly advanced biomolecular NMR. Protein domains, individual residues or certain chemical groups with specific patterns of isotopes can be incorporated to optimize the use of NMR pulse schemes. Here, we describe a novel cell-free protein expression protocol that allows specific isotopic labelling of glycine residues, whilst all other amino acids are independently labelled. This technique enables us to prevent amino acid scrambling and cross-protonation from the solvent resulting in high labelling selectivity of glycine residues as attested by quantification of 15N amide scrambling and residual Ca protonation. We then highlight the potential applications of these samples in the field of biomolecular NMR. We produced a 1 H, 13 C glycine specifically labelled sample of a subunit of the heavy metal ATPase HMA8, in a completely perdeuterated 2 H background and demonstrate how the CH 2 -TROSY experiment recorded on such a sample improves the spectral quality of glycine residues.",
  "abstract_shown": true,
  "affiliations": [
    "Laboratoire Chimie Physique et Chimie du Vivant, CPCV",
    "Sorbonne Université, École Normale Supérieure, PSL Université, CNRS",
    "Integrated Structural Biology Grenoble (ISBG), Cell-free Platform",
    "Univ. Grenoble Alpes, CNRS, CEA, EMBL",
    "Institut de Biologie Structurale (IBS)",
    "Université Grenoble Alpes, CNRS, CEA"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "affs": [
        0,
        1
      ],
      "name": "Rachel Lenoir Capello",
      "orcid": "0000-0003-2225-3167"
    },
    {
      "affs": [
        2,
        3,
        4,
        5
      ],
      "name": "Lionel Imbert",
      "orcid": "0009-0000-6848-7570"
    },
    {
      "affs": [
        4,
        5
      ],
      "name": "Jérôme Boisbouvier",
      "orcid": "0000-0003-3278-3639"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Emeric Miclet",
      "orcid": "0000-0002-6250-1690"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/av4t337p3xjz8.bib",
  "cited_by": 0,
  "doi": "10.26434/chemrxiv.15009868/v1",
  "fulltext_url": null,
  "id": "av4t337p3xjz8",
  "issns": [],
  "landing_url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009868/v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1607|Advanced NMR Techniques and Applications"
    ]
  ],
  "openalex": "W7220463920",
  "pdf_url": "https://chemrxiv.org/doi/pdf/10.26434/chemrxiv.15009868/v1",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-05",
  "publisher": "American Chemical Society (ACS)",
  "ris": "https://research.draconitic.com/paper/av4t337p3xjz8.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:22Z",
      "native_id": "10.26434/chemrxiv.15009868",
      "source": "chemrxiv",
      "url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009868/v1"
    }
  ],
  "subjects": [
    {
      "field": "chemistry",
      "origin": "openalex:1607|Advanced NMR Techniques and Applications",
      "subfield": "physical"
    }
  ],
  "title": "Glycine specifically labelled proteins to enhance solution NMR of methylene groups",
  "title_text": "Glycine specifically labelled proteins to enhance solution NMR of methylene groups",
  "type": "preprint",
  "updated_at": "2026-10-30T12:17:22Z",
  "url": "https://research.draconitic.com/paper/av4t337p3xjz8",
  "venue": "ChemRxiv",
  "versions": []
}