{
  "annotation_id": "06103b08-4048-49f0-9cda-1b66e26f5501",
  "date_created": "2026-03-02T18:01:30.966000Z",
  "date_modified": "2026-03-02T18:01:30.966000Z",
  "file_hash": "c250bd02a7a1f6f8fdd8679faafda5d069b7a91c6850ff6b5da46b0dc4f5d63e",
  "private": false,
  "record": {
    "abstract": "Most proteins involved in processing DNA accomplish their activities as a\nmonomer or as a component of a multimer containing a relatively small number of\nother elements. They generally act locally, binding to one or a few small\nregions of the DNA substrate. Striking exceptions are the \\textit{E. coli}\nprotein RecA and its homologues in other species, whose activities are\nassociated with homologous DNA recombination. The active form of RecA in DNA\nrecombination is a stiff nucleoprotein filament formed by RecA and DNA, within\nwhich the DNA is extended by 50%. Invoking physical and geometrical ideas, we\nshow that the filamentary organization greatly enhances the rate of homologous\nrecognition while preventing the formation of topological traps originating\nfrom multi-site recognition.",
    "arxiv_id": "q-bio/0402008",
    "authors": [
      "Kevin Klapstein",
      "Tom Chou",
      "Robijn Bruinsma"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.stat-mech",
      "q-bio.GN"
    ],
    "doi": "10.1529/biophysj.104.039578",
    "title": "Physics of RecA-mediated homologous recognition",
    "url": "https://arxiv.org/abs/q-bio/0402008"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "31ca2637-5ff5-48f1-afcf-8507284a955e",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}