{
  "annotation_id": "2ed0d78c-99fd-415e-acd1-e5fc6896c826",
  "date_created": "2026-03-02T18:01:32.279000Z",
  "date_modified": "2026-03-02T18:01:32.279000Z",
  "file_hash": "d7ba7fa702574203d8eac9b86c9db829fee0cb52cb6a87b1bb82f2556166131f",
  "private": false,
  "record": {
    "abstract": "We investigate the folding behavior of protein sequences by numerically\nstudying all sequences with maximally compact lattice model through exhaustive\nenumeration. We get the prion-like behavior of protein folding. Individual\nproteins remaining stable in the isolated native state may change their\nconformations when they aggregate. We observe the folding properties as the\ninterfacial interaction strength changes, and find that the strength must be\nstrong enough before the propagation of the most stable structures happens.",
    "arxiv_id": "q-bio/0506012",
    "authors": [
      "Yong-Yun Ji",
      "You-Quan Li",
      "Jun-Wen Mao",
      "Xiao-Wei Tang"
    ],
    "categories": [
      "q-bio.BM"
    ],
    "doi": "10.1103/PhysRevE.72.041912",
    "journal_ref": "Physical Review E 72, 041912 (2005), Virtual Journal of Biological\n  Physics Research(October 15, 2005)",
    "title": "The prion-like folding behavior in aggregated proteins",
    "url": "https://arxiv.org/abs/q-bio/0506012"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "2ff205e1-b2f0-458a-b8ca-238c3a602c18",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}