{
  "annotation_id": "4bedb3dd-5489-4f97-8c25-de0128dcf362",
  "date_created": "2026-03-02T18:00:32.057000Z",
  "date_modified": "2026-03-02T18:00:32.057000Z",
  "file_hash": "4dbe41c6bd37017a86040b824c3bbc7bc40a8bfd51597782d79ddcd04ff16fc4",
  "private": false,
  "record": {
    "abstract": "The folding characteristics of sequences reduced with a possibly simplified\nrepresentation of five types of residues are shown to be similar to their\noriginal ones with the natural set of residues (20 types or 20 letters). The\nreduced sequences have a good foldability and fold to the same native structure\nof their optimized original ones. A large ground state gap for the native\nstructure shows the thermodynamic stability of the reduced sequences. The\ngeneral validity of such a five-letter reduction is further studied via the\ncorrelation between the reduced sequences and the original ones. As a\ncomparison, a reduction with two letters is found not to reproduce the native\nstructure of the original sequences due to its homopolymeric features.",
    "arxiv_id": "physics/0006059",
    "authors": [
      "Jun Wang",
      "Wei Wang"
    ],
    "categories": [
      "physics.bio-ph",
      "q-bio"
    ],
    "doi": "10.1103/PhysRevE.61.6981",
    "journal_ref": "Phys. Rev. E Vol.61, No.6, 6981-6986 (June 2000)",
    "title": "Modeling study on the validity of a possibly simplified representation   of proteins",
    "url": "https://arxiv.org/abs/physics/0006059"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "b4cf45fa-4fa9-430a-bcca-4c82bfd11aeb",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}