{
  "annotation_id": "e0aec02a-bfba-4b7e-ba39-721da29f955f",
  "date_created": "2026-03-02T18:01:31.668000Z",
  "date_modified": "2026-03-02T18:01:31.668000Z",
  "file_hash": "b2a5c8746bf18d781864377c336e6379be429fbb8869d3b62df18df751901248",
  "private": false,
  "record": {
    "abstract": "We present an analysis of the effects of global topology on the structural\nstability of folded proteins in thermal equilibrium with a heat bath. For a\nlarge class of single domain proteins, we computed the harmonic spectrum within\nthe Gaussian Network Model (GNM) and determined the spectral dimension, a\nparameter describing the low frequency behaviour of the density of modes. We\nfind a surprisingly strong correlation between the spectral dimension and the\nnumber of amino acids of the protein. Considering that larger spectral\ndimension value relate to more topologically compact folded state, our results\nindicate that for a given temperature and length of the protein, the folded\nstructure corresponds to the less compact folding compatible with thermodynamic\nstability.",
    "arxiv_id": "q-bio/0405010",
    "authors": [
      "R. Burioni",
      "D. Cassi",
      "F. Cecconi",
      "A. Vulpiani"
    ],
    "categories": [
      "q-bio.BM"
    ],
    "journal_ref": "Proteins 55:529-535 (2004)",
    "title": "Topological thermal instability and length of proteins",
    "url": "https://arxiv.org/abs/q-bio/0405010"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "657ff710-093f-44e7-8779-ad757d7c819e",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}