{
  "meta": {
    "api_type": "NWO Projects API",
    "version": "1.0.2",
    "licence": {
      "name": "CC0 1.0 Universal",
      "url": "https://creativecommons.org/publicdomain/zero/1.0",
      "description": "To the extent possible under law, all copyright and related or neighbouring rights have been waived worldwide to the data made available through this API."
    },
    "documentation": "https://doi.org/10.5281/zenodo.14918287",
    "release_date": "2025-08-20T00:00:00",
    "funder": "https://doi.org/10.13039/501100003246",
    "ror_id": "https://ror.org/04jsz6e67",
    "date": "2026-11-04T00:00:00",
    "count": 1,
    "per_page": 100,
    "pages": 1,
    "page": 1
  },
  "projects": [
    {
      "project_id": "SH-035-08",
      "title": "Autofluorescent proteins in a new light: A quantum Monte Carlo study",
      "funding_scheme_id": 2267,
      "funding_scheme": "Rekentijd nationale computersystemen Rekentijd nationale computersystemen 2008 EW",
      "department": "Exacte en Natuurwetenschappen",
      "sub_department": "Exacte Wetenschappen",
      "start_date": "2007-12-31T00:00:00",
      "end_date": "2009-03-01T00:00:00",
      "reporting_year": 2008,
      "summary_nl": "The project focuses on the accurate quantum Monte Carlo (QMC) computation of the excitation spectra of realistic quantum mechanics in molecular mechanics (QM/MM) protein-chromophore models of the three forms of Green Fluorescent Protein (GFP). It represents the final stage of the previous NCF/SH-035-07 project as the requested computer time will allow us to perform the conclusive set of calculations prior to publication. \n\nUnder the previous NCF project, we have constructed the models of the neutral A, and anionic I and B forms of GFP using density functional theory QM/MM approaches, and demonstrated that TDDFT/MM caculations of the spectra of the GFP protein in its three forms cannot correctly reproduce the experimental shift of the absorption maximum upon deprotonation of the chromophore. Using QMC techniques in the presence of a MM protein environment, we have already performed preliminary calculations of the spectrum of GFP, and found that QMC describes well how the spectrum correlates to the protonation state of the  chromophore. However, the error on the absolute excitation energies is at the moment rather large.\n\nWith the requested computer time, we plan to perform two sets of conclusive studies to really ascertain the performance of QMC in describing the excitations of this autofluorescent protein. We want to enlarge the QM part of the system by including some particular residues which are charged and close to the chromophore as well as employ more sophisticated functional forms for the many-body trial wave functions.",
      "summary_en": "The project focuses on the accurate quantum Monte Carlo (QMC) computation of the excitation spectra of realistic quantum mechanics in molecular mechanics (QM/MM) protein-chromophore models of the three forms of Green Fluorescent Protein (GFP). It represents the final stage of the previous NCF/SH-035-07 project as the requested computer time will allow us to perform the conclusive set of calculations prior to publication. \n\nUnder the previous NCF project, we have constructed the models of the neutral A, and anionic I and B forms of GFP using density functional theory QM/MM approaches, and demonstrated that TDDFT/MM caculations of the spectra of the GFP protein in its three forms cannot correctly reproduce the experimental shift of the absorption maximum upon deprotonation of the chromophore. Using QMC techniques in the presence of a MM protein environment, we have already performed preliminary calculations of the spectrum of GFP, and found that QMC describes well how the spectrum correlates to the protonation state of the  chromophore. However, the error on the absolute excitation energies is at the moment rather large.\n\nWith the requested computer time, we plan to perform two sets of conclusive studies to really ascertain the performance of QMC in describing the excitations of this autofluorescent protein. We want to enlarge the QM part of the system by including some particular residues which are charged and close to the chromophore as well as employ more sophisticated functional forms for the many-body trial wave functions.",
      "project_members": [
        {
          "role": "Project leader",
          "member_id": 135576,
          "last_name": "Filippi",
          "degree_pre_nominal": "prof. dr.",
          "initials": "C.",
          "first_name": "Claudia",
          "organisation": "Universiteit Leiden||Instituut Lorentz Center",
          "organisation_id": 55708,
          "ror": "https://ror.org/027bh9e22",
          "active": false
        },
        {
          "role": "Main Applicant",
          "member_id": 135576,
          "last_name": "Filippi",
          "degree_pre_nominal": "prof. dr.",
          "initials": "C.",
          "first_name": "Claudia",
          "organisation": "Universiteit Twente||Faculty of Science and Technology (TNW)||Applied Physics||Biomolecular Electronic Structure (BES)",
          "organisation_id": 79708,
          "ror": "https://ror.org/006hf6230",
          "active": true
        }
      ]
    }
  ]
}