{
  "annotation_id": "91c26514-6d25-4c6e-b09b-e26835a4bfef",
  "date_created": "2026-03-02T18:01:32.275000Z",
  "date_modified": "2026-03-02T18:01:32.275000Z",
  "file_hash": "bdc6935b9de32a8e2e85767b69b0047d5f6e36270185453a63485141cffd523b",
  "private": false,
  "record": {
    "abstract": "Mechanical unfolding of several domains of calmodulin and titin is studied\nusing a Go-like model with a realistic contact map and Lennard-Jones contact\ninteractions. It is shown that this simple model captures the experimentally\nobserved difference between the two proteins: titin is a spring that is tough\nand strong whereas calmodulin acts like a weak spring with featureless\nforce-displacement curves. The difference is related to the dominance of the\nalpha secondary structures in the native structure of calmodulin. The tandem\narrangements of calmodulin unwind simultaneously in each domain whereas the\ndomains in titin unravel in a serial fashion. The sequences of contact events\nduring unraveling are correlated with the contact order, i.e. with the\nseparation between contact making amino acids along the backbone in the native\nstate. Temperature is found to affect stretching in a profound way.",
    "arxiv_id": "q-bio/0412032",
    "authors": [
      "Marek Cieplak"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.stat-mech"
    ],
    "doi": "10.1016/j.physa.2004.12.032",
    "title": "Mechanical Stretching of Proteins: Calmodulin and Titin",
    "url": "https://arxiv.org/abs/q-bio/0412032"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "30da0c50-9519-4657-bde4-6edbbb920e0d",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}