Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/5746
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dc.contributor.authorNsiah, Francis-
dc.contributor.authorMcDermott, Mark T.-
dc.date.accessioned2021-07-27T10:05:59Z-
dc.date.available2021-07-27T10:05:59Z-
dc.date.issued2015-
dc.identifier.issn23105496-
dc.identifier.urihttp://hdl.handle.net/123456789/5746-
dc.description21p:, ill.en_US
dc.description.abstractThe adsorption characteristics of human fibrinogen (HFG) on surfaces with well-controlled chemistries have been studied using infrared reflection absorption spectroscopy. The surfaces examined in this study provide the experimental basis for exploring fundamental non-covalent intermolecular forces that dominate protein adsorption processes. Comparisons were drawn between fibrinogen and non-specifically adsorbed bovine IgG (bIgG) as well as structurally rigid lysozyme (LYS) on a positively-charged amine-modified surface to further understand substrate-influence on protein surface coverage. Work presented herein shows that surface coverage of an adsorbed protein depends largely on the nature of the substrate and the protein structureen_US
dc.language.isoenen_US
dc.publisherUniversity of Cape Coasten_US
dc.subjectProtein adsorptionen_US
dc.subjectFibrinogenen_US
dc.subjectInfrared reflection absorption spectroscopyen_US
dc.subjectGold substrate21en_US
dc.titleInvestigation of adsorption characteristics of fibrinogen on modified gold substrates using infrared reflection absorption spectroscopyen_US
dc.typeArticleen_US
Appears in Collections:Department of Chemistry

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