{
  "abstract": "The structural \\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$\\beta \\gamma$$\\end{document}-crystallin from the tunicate Ciona intestinalis serves as an evolutionary waypoint between ancestral metal cation-binding crystallins and the \\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$\\beta \\gamma$$\\end{document} crystallins of the vertebrate eye lens. Ci-\\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$\\beta \\gamma$$\\end{document} maintains the metal cation-binding sites of ancestral crystallins while also sharing common structural motifs with vertebrate lens crystallins. Due to its structure and strong interaction with Ca\\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$^{2+}$$\\end{document}, Ci-\\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$\\beta \\gamma$$\\end{document} is more thermally and chemically stable than vertebrate lens crystallins, making it an ideal starting point for understanding \\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$\\beta \\gamma$$\\end{document} crystallins’ evolution for molecular stability. In this study, we present the side-chain and updated backbone resonance assignments of Ci-\\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$\\beta \\gamma$$\\end{document} with TALOS-N predictions on the H\\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$_N$$\\end{document}, H\\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$_\\alpha$$\\end{document}, C\\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$_\\alpha$$\\end{document}, C\\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$_\\beta$$\\end{document} and N chemical shifts. These assignments provide a foundation for future studies of metal binding, dynamics, and stability of proteins in the \\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$\\beta \\gamma$$\\end{document}-crystallin family.",
  "abstract_shown": true,
  "affiliations": [
    "Department of Chemistry, University of California, Irvine, 1102 Natural Sciences 2, Irvine, 92697-2025 CA United States of America",
    "Department of Molecular Biology and Biochemistry, University of California, Irvine, McGaugh Hall, Irvine, 92697-3900 CA United States of America",
    "Department of Ophthalmology and Visual Sciences, Gavin Herbert Eye Institute, University of California, Irvine, CA 92617 Irvine, United States of America"
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 6,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Matthew D. Jimenez"
    },
    {
      "affs": [
        0
      ],
      "name": "Mina Mozafari"
    },
    {
      "affs": [
        0
      ],
      "name": "Cat Tuong Nguyen Hoang"
    },
    {
      "affs": [
        0
      ],
      "name": "Miram Ali Al-Botaif"
    },
    {
      "affs": [
        0
      ],
      "name": "Jeongwoo Ko"
    },
    {
      "affs": [
        0,
        1,
        2
      ],
      "name": "Rachel W. Martin",
      "orcid": "0000-0001-9996-7411"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/bxnetjrwfb7w8.bib",
  "cited_by": 0,
  "doi": "10.1007/s12104-026-10280-7",
  "fulltext_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC13724631/",
  "id": "bxnetjrwfb7w8",
  "issns": [
    "1874-2718",
    "1874-270X"
  ],
  "landing_url": "https://doi.org/10.1007/s12104-026-10280-7",
  "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",
      "Article"
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    [
      "openalex",
      "1312|Protein Structure and Dynamics"
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  "openalex": "W7225046323",
  "pdf_url": "https://link.springer.com/content/pdf/10.1007/s12104-026-10280-7.pdf",
  "pmcid": "PMC13724631",
  "pmid": "42967260",
  "published": "2026-11-01",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/bxnetjrwfb7w8.ris",
  "sources": [
    {
      "first_seen": "2026-11-04T12:23:10Z",
      "native_id": "PMC13724631",
      "source": "pmc",
      "url": "https://doi.org/10.1007/s12104-026-10280-7"
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  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Protein Structure and Dynamics",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Backbone and side-chain NMR resonance assignments of Ciona intestinalis\\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}$$\\beta \\gamma$$\\end{document}-crystallin",
  "title_text": "Backbone and side-chain NMR resonance assignments of Ciona intestinalis\\documentclass[12pt]{minimal} \\usepackage{amsmath} \\usepackage{wasysym} \\usepackage{amsfonts} \\usepackage{amssymb} \\usepackage{amsbsy} \\usepackage{mathrsfs} \\usepackage{upgreek} \\setlength{\\oddsidemargin}{-69pt} \\begin{document}β γ\\end{document}-crystallin",
  "type": "peer-reviewed",
  "updated_at": "2026-11-06T12:21:03Z",
  "url": "https://research.draconitic.com/paper/bxnetjrwfb7w8",
  "venue": "Biomolecular Nmr Assignments",
  "versions": []
}