{
  "annotation_id": "07600794-eff9-498b-a850-177d2a520085",
  "date_created": "2026-03-02T18:01:30.959000Z",
  "date_modified": "2026-03-02T18:01:30.959000Z",
  "file_hash": "bbc5c95380b5888f0b69c250f31d7ae519af5d18d7762459baea2b743d7b5102",
  "private": false,
  "record": {
    "abstract": "Using a simple hydrophobic/polar protein model, we perform a Monte Carlo\nstudy of the thermodynamics and kinetics of binding to a target structure for\ntwo closely related sequences, one of which has a unique folded state while the\nother is unstructured. We obtain significant differences in their binding\nbehavior. The stable sequence has rigid docking as its preferred binding mode,\nwhile the unstructured chain tends to first attach to the target and then fold.\nThe free-energy profiles associated with these two binding modes are compared.",
    "arxiv_id": "q-bio/0312048",
    "authors": [
      "Nitin Gupta",
      "Anders Irb\u00e4ck"
    ],
    "categories": [
      "q-bio.BM",
      "cond-mat.soft"
    ],
    "doi": "10.1063/1.1643900",
    "journal_ref": "J. Chem. Phys. 120 (2004) 3983-3989",
    "title": "Coupled folding-binding versus docking: A lattice model study",
    "url": "https://arxiv.org/abs/q-bio/0312048"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "c6d04ffe-0171-4525-835b-6d46dcf3c3bb",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}