{
  "annotation_id": "79722f76-6ffa-4442-802a-694bbd8c9513",
  "date_created": "2026-03-02T18:01:31.809000Z",
  "date_modified": "2026-03-02T18:01:31.809000Z",
  "file_hash": "0f9dc83db92268e379a37c5556700e263040f6c85255e85762bec304439b8884",
  "private": false,
  "record": {
    "abstract": "Structure predictions of helical membrane proteins have been designed to take\nadvantage of the structural autonomy of secondary structure elements, as\npostulated by the two-stage model of Engelman and Popot. In this context, we\ninvestigate structure calculation strategies for two membrane proteins with\ndifferent functions, sizes, aminoacid compositions, and topologies: the\nglycophorin A homodimer (a paradigm for close inter-helical packing in membrane\nproteins) and aquaporin (a channel protein). Our structure calculations are\nbased on two alternative folding schemes: a one-step simulated annealing from\nan extended chain conformation, and a two-step procedure inspired by the\ngrid-search methods traditionally used in membrane protein predictions. In this\nframework, we investigate rationales for the utilization of sparse NMR data\nsuch as distance-based restraints and residual dipolar couplings in structure\ncalculations of helical membrane proteins.",
    "arxiv_id": "q-bio/0505014",
    "authors": [
      "Ileana Stoica"
    ],
    "categories": [
      "q-bio.BM"
    ],
    "title": "Structure calculation strategies for helical membrane proteins; a   comparison study",
    "url": "https://arxiv.org/abs/q-bio/0505014"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "fa9d2347-fcad-4c1f-a64a-0452b8ff15dc",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}