{
  "annotation_id": "b03a6bb5-b2f4-4b04-97ec-e636336395d4",
  "date_created": "2026-03-02T18:01:35.709000Z",
  "date_modified": "2026-03-02T18:01:35.709000Z",
  "file_hash": "c1aab4bed15e6d63b5faaeabe74031a160dd8f629d16369b8ec0fb876dc364ac",
  "private": false,
  "record": {
    "abstract": "We investigate aggregation mechanism of two proteins in a thermodynamically\nunambiguous manner by considering the finite size effect of free energy\nlandscape of HP lattice protein model. Multi-Self-Overlap-Ensemble Monte Carlo\nmethod is used for numerical calculations. We find that a dimer can be formed\nspontaneously as a thermodynamically stable state when the system is small\nenough. It implies the possibility that the aggregation of proteins in a cell\nis triggered when they are confined in a small region by, for example, being\nsurrounded by other macromolecules.We also find that the dimer exhibits a\ntransition between unstable state and metastable state in the infinite system.",
    "arxiv_id": "q-bio/0603024",
    "authors": [
      "Kazuki Nakanishi",
      "Macoto Kikuchi"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.soft"
    ],
    "doi": "10.1143/JPSJ.75.064803",
    "title": "Thermodynamics of aggregation of two proteins",
    "url": "https://arxiv.org/abs/q-bio/0603024"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "5b0ac6dc-3005-420b-8786-1bb0501ae855",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}