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<>
	foaf:primaryTopic <http://crdd.osdd.net/open/id/eprint/3232>;
	rdfs:comment "The repository administrator has not yet configured an RDF license."^^xsd:string .

<http://crdd.osdd.net/open/3232/>
	dc:format "text/html";
	dc:title "HTML Summary of #3232 \n\nDeciphering the underlying mechanism for Au/ZnO nanocomposites-induced modulation of structural features and thermodynamic stability of horse myoglobin\n\n";
	foaf:primaryTopic <http://crdd.osdd.net/open/id/eprint/3232> .

<http://crdd.osdd.net/open/id/eprint/3232#authors>
	rdf:_1 <http://crdd.osdd.net/open/id/person/ext-b71b5705218c793445bc50702eaf5737>;
	rdf:_2 <http://crdd.osdd.net/open/id/person/ext-86cdcdffb05761c813de490c4cde3a8f>;
	rdf:_3 <http://crdd.osdd.net/open/id/person/ext-ec5e6650596f523e5c0ad259f1d6052c>;
	rdf:_4 <http://crdd.osdd.net/open/id/person/ext-cb3d11b6d82a154cf7298c39206ace52> .

<http://crdd.osdd.net/open/id/eprint/3232>
	bibo: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."^^xsd:string;
	bibo:authorList <http://crdd.osdd.net/open/id/eprint/3232#authors>;
	bibo:issue "19";
	bibo:volume "41";
	dct:creator <http://crdd.osdd.net/open/id/person/ext-86cdcdffb05761c813de490c4cde3a8f>,
		<http://crdd.osdd.net/open/id/person/ext-b71b5705218c793445bc50702eaf5737>,
		<http://crdd.osdd.net/open/id/person/ext-cb3d11b6d82a154cf7298c39206ace52>,
		<http://crdd.osdd.net/open/id/person/ext-ec5e6650596f523e5c0ad259f1d6052c>;
	dct:date "2025-05";
	dct:isPartOf <http://crdd.osdd.net/open/id/repository>,
		<http://crdd.osdd.net/open/id/publication/ext-c6c1275231b30f33dfaa5c56e674ac92>;
	dct:publisher <http://crdd.osdd.net/open/id/org/ext-9b1c5880a971a08da83400605a5e8c13>;
	dct:title "Deciphering the underlying mechanism for Au/ZnO nanocomposites-induced modulation of structural features and thermodynamic stability of horse myoglobin"^^xsd:string;
	rdf:type bibo:AcademicArticle,
		bibo:Article,
		ep:ArticleEPrint,
		ep:EPrint;
	rdfs:seeAlso <http://crdd.osdd.net/open/3232/> .

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	foaf:name "American Chemical Society (ACS)"^^xsd:string;
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	foaf:familyName "Sharma"^^xsd:string;
	foaf:givenName "Deepak"^^xsd:string;
	foaf:name "Deepak Sharma"^^xsd:string;
	rdf:type foaf:Person .

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	foaf:familyName "Kaur"^^xsd:string;
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	foaf:name "Kiranjot Kaur"^^xsd:string;
	rdf:type foaf:Person .

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	foaf:givenName "Rajesh"^^xsd:string;
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	foaf:familyName "Haldar"^^xsd:string;
	foaf:givenName "Krishna Kanta"^^xsd:string;
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	foaf:name "Langmuir"^^xsd:string;
	rdf:type bibo:Collection .

