{
  "annotation_id": "9df672d7-6b1a-43d9-96a1-5062680caf41",
  "date_created": "2026-03-02T18:01:32.281000Z",
  "date_modified": "2026-03-02T18:01:32.281000Z",
  "file_hash": "6cd9a4fa3878e574f707ac378c46692d98676f034da3b634e139b885187880fc",
  "private": false,
  "record": {
    "abstract": "We study the medium effects on the selection of sequences in protein folding\nby taking account of the surface potential in HP-model. Our analysis on the\nproportion of H and P monomers in the sequences gives a direct interpretation\nthat the lowly designable structures possess small average gap. The numerical\ncalculation by means of our model exhibits that the surface potential enhances\nthe average gap of highly designable structures. It also shows that a most\nstable structure may be no longer the most stable one if the medium parameters\nchanged.",
    "arxiv_id": "q-bio/0408024",
    "authors": [
      "You-Quan Li",
      "Yong-Yun Ji",
      "Jun-Wen Mao",
      "Xiao-Wei Tang"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.soft"
    ],
    "doi": "10.1103/PhysRevE.72.021904",
    "journal_ref": "Phys. Rev. E 72, 021904 (2005)",
    "title": "Medium effects on the selection of sequences folding into stable   proteins in a simple model",
    "url": "https://arxiv.org/abs/q-bio/0408024"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "9d718ffe-6bec-4085-8e61-8e2d4993b0f1",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}