{
  "annotation_id": "b8fec70c-442c-462c-b949-1f3df8d5140e",
  "date_created": "2026-03-02T18:00:39.432000Z",
  "date_modified": "2026-03-02T18:00:39.432000Z",
  "file_hash": "3159a463cb5eecf5d6f391d34a201a40b335ae4d62abf53b44959c09a5838ae8",
  "private": false,
  "record": {
    "abstract": "A lattice based model of a protein is used to study the dimerization\nequilibrium of the GCN4 leucine zipper. Replica exchange Monte Carlo is used to\ndetermine the free energy of both the monomeric and dimeric forms as a function\nof temperature. The method of coincidences is then introduced to explicitly\ncalculate the entropy loss associated with dimerization, and from it the free\nenergy difference between monomer and dimer, as well as the corresponding\nequilibrium reaction constant. We find that the entropy loss of dimerization is\na strong function of energy (or temperature), and that it is much larger than\npreviously estimated, especially for high energy states. The results confirm\nthat it is possible to study the dimerization equilibrium of GCN4 at\nphysiological concentrations within the reduced representation of the protein\nemployed.",
    "arxiv_id": "physics/0204006",
    "authors": [
      "Jorge Vinals",
      "Andrzej Kolinski",
      "Jeffrey Skolnick"
    ],
    "categories": [
      "physics.bio-ph",
      "q-bio.BM"
    ],
    "doi": "10.1016/S0006-3495(02)75289-2",
    "journal_ref": "Biophys. J. 83, 2801 (2002).",
    "title": "Numerical estimation of entropy loss on dimerization: improved   prediction of the quaternary structure of the GCN4 leucine zipper",
    "url": "https://arxiv.org/abs/physics/0204006"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "db1b6337-8353-4edf-b8d9-0637ed39d5fa",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}