{
  "abstract": "Biomolecular condensation emerges from networks of multivalent interactions that respond collectively to molecular composition and environmental conditions. Here, we establish a sequential Design of Experiments (DoE) framework to systematically and efficiently characterise multidimensional condensation landscapes. Applied to three RNA-binding condensate proteins - Dhh1, Ded1 and PGL-3 - the workflow revealed unexpected protein-specific interactions between biophysical and biochemical variables, including RNA, pH and ionic strength, and uncovered context-dependent switch-like behaviours. Extending the framework to protein mixtures revealed how proteins affected each other's condensation and whether they formed condensate-within-condensate structures under different experimental conditions. Finally, an unexpected response identified by DoE prompted mechanistic analysis of Dhh1, revealing an ATP-independent RNA-binding surface that promotes efficient condensation in vitro and contributes to P-body formation in cells. Sequential DoE therefore provides an experimentally accessible strategy for uncovering context-dependent condensate regulation and converting multidimensional response patterns into mechanistic hypotheses.",
  "abstract_shown": true,
  "affiliations": [
    "Biozentrum, University of Basel, Basel, Switzerland"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "name": "M. Siketanc"
    },
    {
      "name": "F. Weidner"
    },
    {
      "name": "C. M. Nuesperling"
    },
    {
      "affs": [
        0
      ],
      "name": "M. Hondele"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/ez9y2jmwaedp5.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.29.755056",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.29.755056v1.full",
  "id": "ez9y2jmwaedp5",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.29.755056v1",
  "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|RNA Research and Splicing"
    ]
  ],
  "openalex": "W7215123775",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.29.755056v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-29",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/ez9y2jmwaedp5.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:25:39Z",
      "native_id": "10.64898/2026.09.29.755056",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.29.755056v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Sequential Design of Experiments enables accessible and efficient multidimensional mapping of single- and multi-protein condensates",
  "title_text": "Sequential Design of Experiments enables accessible and efficient multidimensional mapping of single- and multi-protein condensates",
  "type": "preprint",
  "updated_at": "2026-10-30T12:25:39Z",
  "url": "https://research.draconitic.com/paper/ez9y2jmwaedp5",
  "venue": "bioRxiv",
  "versions": []
}