{
  "annotation_id": "15bfb684-bb6f-4961-993d-aad4d78c9e4e",
  "date_created": "2026-03-02T18:00:45.964000Z",
  "date_modified": "2026-03-02T18:00:45.964000Z",
  "file_hash": "4511b2733980ff73a4bc6bf8947daed60b7e692101e59fe3986d6ea9eb1bee64",
  "private": false,
  "record": {
    "abstract": "We report the reproducible first-principles folding of the 40 amino acid,\nthree-helix headpiece of the HIV accessory protein in a recently developed\nall-atom free-energy forcefield. Six of twenty simulations using an adapted\nbasin-hopping method converged to better than 3 \\AA backbone RMS deviation to\nthe experimental structure. Using over 60,000 low-energy conformations of this\nprotein, we constructed a decoy tree that completely characterizes its folding\nfunnel.",
    "arxiv_id": "physics/0310146",
    "authors": [
      "T. Herges",
      "W. Wenzel"
    ],
    "categories": [
      "physics.bio-ph",
      "physics.comp-ph",
      "q-bio.BM"
    ],
    "title": "In-silico folding of a three helix protein and characterization of its   free-energy landscape in an all-atom forcefield",
    "url": "https://arxiv.org/abs/physics/0310146"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "d1f5961f-878e-4fa8-aef5-75145434ca32",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}