{
  "abstract": "All-atom simulations with explicit solvent can provide a detailed and accurate description of dynamics and mechanisms in biomolecular systems, including intrinsically disordered proteins (IDPs) and their condensates. However, interactions involving charged residues and ions remain a persistent source of systematic error. Here we introduce an osmometry-guided optimization strategy that directly targets residue-residue, residue-ion and ion-ion interactions. Osmotic pressure provides key experimental information on molecular interactions and can be calculated directly and rapidly from simulations, enabling iterative force-field optimization. The resulting parameters improve agreement with single-molecule FRET data for IDPs, NMR relaxation data for an IDP-folded-domain complex, and chain dynamics and dimensions in biomolecular condensates of charged IDPs. For such condensates, simulations with our osmometry-optimized force field provide the missing link for predicting condensate dynamics across length and time scales. The strategy is broadly extensible to other interaction classes, including those governing protein-nucleic-acid assemblies.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "name": "M. T. Ivanovic"
    },
    {
      "name": "V. von Roten"
    },
    {
      "name": "B. Schuler"
    },
    {
      "name": "R. B. Best"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/aqka3ntby2jkc.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.08.25.747127",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.08.25.747127v2.full",
  "id": "aqka3ntby2jkc",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.08.25.747127v2",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biophysics"
    ],
    [
      "openalex",
      "1312|Protein Structure and Dynamics"
    ]
  ],
  "openalex": "W7204491390",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.08.25.747127v2.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-08-25",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/aqka3ntby2jkc.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:22:31Z",
      "native_id": "10.64898/2026.08.25.747127",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.08.25.747127v2"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Predictive all-atom simulations of disordered proteins and biomolecular condensates through osmometry-guided force-field optimization",
  "title_text": "Predictive all-atom simulations of disordered proteins and biomolecular condensates through osmometry-guided force-field optimization",
  "type": "preprint",
  "updated_at": "2026-10-30T12:22:31Z",
  "url": "https://research.draconitic.com/paper/aqka3ntby2jkc",
  "venue": "bioRxiv",
  "versions": []
}