{
  "abstract": "We present a new method to evaluate the two-body partition function and related thermodynamic properties using a discrete grid of angles between molecular bodies. The method, based on subdivided spheres, is applied to protein-protein interactions, which depend on their separation, as well as relative orientations. Orientational dependence is due to force anisotropies, which are reflected in thermody- namic quantities. Non-monotonic variations, with both ionic strength and temperature, are shown for the osmotic second virial coefficient (B2); a widely used metric for assessing protein stability in pharmaceutical formulations. Variations of the Calvados3 force-field were applied on α-Chymotrypsinogen A, “Cgn”, showing that to capture the non-monotonic variations at low salt, the amino acid charges have to be placed off-center. This correction renders results matching presented experimental data, see Fig. 3. A principal component analysis (PCA) found configurational clusters at free energy minima, some of which we could match to empirical structures. The method is implemented in an open source computa- tional tool, Duello, for analyzing arbitrary molecules, including globular proteins. Our technique systematically explores and discretizes angular space on a nearly spherically-uniform grid, enabling efficient calculations of the two-body partition function and, subsequently, all related thermodynamic quantities. Where available, excellent agreement is found with experiment and exact numerical simulations.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 6,
  "authors": [
    {
      "name": "Isabel Vinterbladh"
    },
    {
      "name": "Jordan Bye"
    },
    {
      "name": "Robin Curtis"
    },
    {
      "name": "Harold W. Hatch"
    },
    {
      "name": "Sergei Grudinin"
    },
    {
      "name": "Mikael Lund"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/8eczt9p941pt2.bib",
  "cited_by": 1,
  "doi": "10.1021/acs.jpcb.6c01665",
  "fulltext_url": null,
  "id": "8eczt9p941pt2",
  "issns": [
    "1520-6106",
    "1520-5207"
  ],
  "landing_url": "https://hal.science/hal-05337856v2",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.chim"
    ],
    [
      "hal",
      "0.phys"
    ],
    [
      "hal",
      "1.chim.theo"
    ],
    [
      "hal",
      "1.phys.phys"
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    [
      "hal",
      "2.phys.phys.phys-bio-ph"
    ],
    [
      "hal",
      "2.phys.phys.phys-comp-ph"
    ],
    [
      "openalex",
      "1606|Advanced Physical and Chemical Molecular Interactions"
    ]
  ],
  "openalex": "W7163995225",
  "pdf_url": "https://hal.science/hal-05337856/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-06-09",
  "publisher": "American Chemical Society",
  "ris": "https://research.draconitic.com/paper/8eczt9p941pt2.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:01Z",
      "native_id": "hal-05337856",
      "source": "hal",
      "url": "https://hal.science/hal-05337856v2"
    }
  ],
  "subjects": [
    {
      "field": "chemistry",
      "origin": "hal:1.chim.theo",
      "subfield": "theoretical"
    },
    {
      "field": "physics",
      "origin": "hal:2.phys.phys.phys-bio-ph",
      "subfield": "biological-medical"
    },
    {
      "field": "physics",
      "origin": "hal:2.phys.phys.phys-comp-ph",
      "subfield": "computational"
    }
  ],
  "title": "Intermolecular Pose Exploration using Subdivided Spheres",
  "title_text": "Intermolecular Pose Exploration using Subdivided Spheres",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:18:01Z",
  "url": "https://research.draconitic.com/paper/8eczt9p941pt2",
  "venue": "Journal of Physical Chemistry B",
  "versions": []
}