{
  "abstract": "Bacterial ice-nucleating proteins (INPs) are known as the most efficient biological heterogeneous ice nucleators. Ice-nucleation ability is conventionally attributed to the threonine-based conserved motifs of {beta} -helical INPs, whereas the role of other conserved motifs remains overlooked. To identify the motif with the highest hydration-ordering ability, a 16-loop model INP and its two mutants are simulated using all-atom molecular dynamics at 260 K, just below the ice nucleation temperature, using the CHARMM36m force field and TIP4P/Ice water model. Among four potential ice-nucleating sites present in four exposed surfaces of the {beta} -helical INP, the glycine-tyrosine-glycine (GYG) motif-associated interface water (IW) exhibits the probability distribution of the Steinhardt bond-orientational and tetrahedral order parameters closest to that of the Ih. The GYG arrange themselves into a ladder-like array of tyrosine hydroxyls, compatible with the Ih-like lattice geometry, suggesting that this motif provides the IW a favorable template for ice-like water organization. The Y-to-phenylalanine mutation produces the largest disruption in IW order compared to the threonine mutations. Although the difference in entropy of threonine-associated IW and Ih is the least among all sites, ice-like hydration ordering near GYG may exceed prior assumptions for a threonine-based ice-nucleating surface. The ordering is collectively determined by lattice compatibility, entropy reduction, hydrophobicity, interfacial geometry, and sequence conservation. The study unfolds a molecular framework of biological ice nucleation and provides a foundation for the rational engineering of more efficient artificial ice-nucleators for applications in climate-related technologies.",
  "abstract_shown": true,
  "affiliations": [
    "Indian Institute of Technology, Jodhpur"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 2,
  "authors": [
    {
      "name": "S. E. Jadhav"
    },
    {
      "affs": [
        0
      ],
      "name": "A. Debnath"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/ehk15rdjqadd3.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.15.759343",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.15.759343v1.full",
  "id": "ehk15rdjqadd3",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.15.759343v1",
  "language": null,
  "licence": "CC-BY-NC",
  "licence_label": "CC BY-NC",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biophysics"
    ],
    [
      "openalex",
      "1902|nanoparticles nucleation surface interactions"
    ]
  ],
  "openalex": "W7222608865",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.15.759343v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-15",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/ehk15rdjqadd3.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:28:07Z",
      "native_id": "10.64898/2026.10.15.759343",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.15.759343v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Nanoscopic Origin of Enhanced Tyrosine-Mediated Water Ordering over Canonical Threonine Motifs in a Bacterial Ice-Nucleating Protein",
  "title_text": "Nanoscopic Origin of Enhanced Tyrosine-Mediated Water Ordering over Canonical Threonine Motifs in a Bacterial Ice-Nucleating Protein",
  "type": "preprint",
  "updated_at": "2026-10-30T12:28:07Z",
  "url": "https://research.draconitic.com/paper/ehk15rdjqadd3",
  "venue": "bioRxiv",
  "versions": []
}