{
      "number": 19,
      "eprintid": 3232,
      "date": "2025-05",
      "userid": 2,
      "rev_number": 3,
      "creators": [
        {
          "name": {
            "lineage": null,
            "given": "Kiranjot",
            "honourific": null,
            "family": "Kaur"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Deepak",
            "honourific": null,
            "family": "Sharma"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Krishna Kanta",
            "honourific": null,
            "family": "Haldar"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Rajesh",
            "honourific": null,
            "family": "Kumar"
          }
        }
      ],
      "dir": "disk0\/00\/00\/32\/32",
      "lastmod": "2026-02-01 14:14:09",
      "pagerange": "12008-12021",
      "publisher": "American Chemical Society (ACS)",
      "metadata_visibility": "show",
      "eprint_status": "archive",
      "status_changed": "2026-02-01 14:14:09",
      "volume": 41,
      "datestamp": "2026-02-01 14:14:09",
      "uri": "http:\/\/crdd.osdd.net\/open\/id\/eprint\/3232",
      "type": "article",
      "title": "Deciphering the underlying mechanism for Au\/ZnO nanocomposites-induced modulation of structural features and thermodynamic stability of horse myoglobin",
      "abstract": "Au\/ZnO nanocomposites (NCs) were synthesized and characterized by using various analytical techniques. Analysis of Au\/ZnO NCs effect on 1H NMR, CD, fluorescence, and absorbance spectra of horse myoglobin (h-Mb) at 0.0 and 5.0 M urea (pH 7.4) revealed that the Au\/ZnO NCs weaken the heme-globin interactions and also disrupt the secondary\/tertiary structure of h-Mb. Furthermore, the Au\/ZnO NCs effect of weakening the heme-globin interactions and disrupting the protein structures was detected more in the denaturant media than in the aqueous solution. Analysis of the Au\/ZnO NCs effect on thermodynamic parameters (based on absorbance at 409 nm, CD at 222 nm, and DSC) of h-Mb at pH 7.4 revealed that the Au\/ZnO NCs decrease the thermodynamic stability of h-Mb. Investigation of Au\/ZnO NC's effects on urea concentration-dependent unfolding free energy of h-Mb at pH 7.4 showed that the Au\/ZnO NCs strengthen the urea impact to decrease the thermodynamic stability of h-Mb. The quantitative estimation of enthalpic and entropic contributions to the Au\/ZnO NCs-mediated decrease in the unfolding free energy of h-Mb reveals that the Au\/ZnO NCs decrease the local (heme-globin interactions) and structural thermodynamic stability of the protein due to the enthalpic interactions of h-Mb with Au\/ZnO NCs. ITC and time-resolved fluorescence studies of h-Mb further suggest that the Au\/ZnO NCs form binding interactions with h-Mb at pH 7.4.",
      "publication": "Langmuir"
    }