<mets:mets OBJID="eprint_3232" LABEL="Eprints Item" xsi:schemaLocation="http://www.loc.gov/METS/ http://www.loc.gov/standards/mets/mets.xsd http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-3.xsd" xmlns:mets="http://www.loc.gov/METS/" xmlns:mods="http://www.loc.gov/mods/v3" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance"><mets:metsHdr CREATEDATE="2026-07-25T23:11:31Z"><mets:agent ROLE="CUSTODIAN" TYPE="ORGANIZATION"><mets:name>open</mets:name></mets:agent></mets:metsHdr><mets:dmdSec ID="DMD_eprint_3232_mods"><mets:mdWrap MDTYPE="MODS"><mets:xmlData><mods:titleInfo><mods:title>Deciphering the underlying mechanism for Au/ZnO nanocomposites-induced modulation of structural features and thermodynamic stability of horse myoglobin</mods:title></mods:titleInfo><mods:name type="personal"><mods:namePart type="given">Kiranjot</mods:namePart><mods:namePart type="family">Kaur</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart type="given">Deepak</mods:namePart><mods:namePart type="family">Sharma</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart type="given">Krishna Kanta</mods:namePart><mods:namePart type="family">Haldar</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart type="given">Rajesh</mods:namePart><mods:namePart type="family">Kumar</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods: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.</mods:abstract><mods:originInfo><mods:dateIssued encoding="iso8061">2025-05</mods:dateIssued></mods:originInfo><mods:originInfo><mods:publisher>American Chemical Society (ACS)</mods:publisher></mods:originInfo><mods:genre>Article</mods:genre></mets:xmlData></mets:mdWrap></mets:dmdSec><mets:amdSec ID="TMD_eprint_3232"><mets:rightsMD ID="rights_eprint_3232_mods"><mets:mdWrap MDTYPE="MODS"><mets:xmlData><mods:useAndReproduction>
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