{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8"],"submitter":["Javkhlantugs N"],"pubmed_abstract":["Having a theoretical understanding of the orientation of immunoglobulin on an immobilized solid surface is important in biomedical pathogen-detecting systems and cellular analysis. Despite the stable adsorption of immunoglobulin on a polystyrene (PS) surface that has been applied in many kinds of immunoassays, there are many uncertainties in antibody-based clinical and biological experimental methods. To understand the binding mechanism and physicochemical interactions between immunoglobulin and the PS surface at the atomic level, we investigated the binding behavior and interactions of the monoclonal immunoglobulin G (IgG) on the PS surface using the computational method. In our docking simulation with the different arrangement of translational and rotational orientation of IgG onto the P"],"journal":["International journal of nanomedicine"],"pagination":["2487-96"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3713897"],"repository":["biostudies-literature"],"pubmed_title":["Computational study on the interactions and orientation of monoclonal human immunoglobulin G on a polystyrene surface."],"pmcid":["PMC3713897"],"pubmed_authors":["Ueda K","Javkhlantugs N","Bayar H","Ganzorig C"],"additional_accession":[]},"is_claimable":false,"name":"Computational study on the interactions and orientation of monoclonal human immunoglobulin G on a polystyrene surface.","description":"Having a theoretical understanding of the orientation of immunoglobulin on an immobilized solid surface is important in biomedical pathogen-detecting systems and cellular analysis. Despite the stable adsorption of immunoglobulin on a polystyrene (PS) surface that has been applied in many kinds of immunoassays, there are many uncertainties in antibody-based clinical and biological experimental methods. To understand the binding mechanism and physicochemical interactions between immunoglobulin and the PS surface at the atomic level, we investigated the binding behavior and interactions of the monoclonal immunoglobulin G (IgG) on the PS surface using the computational method. In our docking simulation with the different arrangement of translational and rotational orientation of IgG onto the P","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013","modification":"2026-06-15T03:22:27.551Z","creation":"2026-06-15T03:12:17.042Z"},"accession":"S-EPMC3713897","cross_references":{"pubmed":["23874096"],"doi":["10.2147/IJN.S44479"]}}