{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8(33)"],"submitter":["Ahmed I"],"pubmed_abstract":["In the present study, the intermolecular interactions between a water-insoluble phospholipid (DOPC) and water-soluble protein (myoglobin) and the interaction among themselves were investigated at the air-water interface using the Langmuir and Langmuir-Blodgett techniques. The effects of changes in physicochemical factors, like pH and temperature, on these interactions were also examined. Surface pressure-molecular area (π-<i>A</i>) isotherms of the DOPC monolayer at the air-water interface, with and without myoglobin (Myo) revealed the evolution of various physical properties, such as elastic, thermodynamic, and hysteric properties, in response to changes in subphase pH and temperature. With the increment of subphase pH from 5 to 7 at a fixed temperature (20 °C), the DOPC isotherm expanded"],"journal":["ACS omega"],"pagination":["30199-30212"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10448488"],"repository":["biostudies-literature"],"pubmed_title":["Interfacial Interactions of a Myoglobin/DOPC Hybrid System at the Air-Water Interface and Its Physicochemical Properties."],"pmcid":["PMC10448488"],"pubmed_authors":["Islam AKMM","Ahmed I","Das N","Plaisier JR","Bal JK","Parisse P"],"additional_accession":[]},"is_claimable":false,"name":"Interfacial Interactions of a Myoglobin/DOPC Hybrid System at the Air-Water Interface and Its Physicochemical Properties.","description":"In the present study, the intermolecular interactions between a water-insoluble phospholipid (DOPC) and water-soluble protein (myoglobin) and the interaction among themselves were investigated at the air-water interface using the Langmuir and Langmuir-Blodgett techniques. The effects of changes in physicochemical factors, like pH and temperature, on these interactions were also examined. Surface pressure-molecular area (π-<i>A</i>) isotherms of the DOPC monolayer at the air-water interface, with and without myoglobin (Myo) revealed the evolution of various physical properties, such as elastic, thermodynamic, and hysteric properties, in response to changes in subphase pH and temperature. With the increment of subphase pH from 5 to 7 at a fixed temperature (20 °C), the DOPC isotherm expanded","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Aug","modification":"2025-04-19T23:18:33.363Z","creation":"2025-04-19T23:18:33.363Z"},"accession":"S-EPMC10448488","cross_references":{"pubmed":["37636970"],"doi":["10.1021/acsomega.3c02909"]}}