Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3852
DC FieldValueLanguage
dc.contributor.authorR., Barbuccien_us
dc.contributor.authorMagnani, Agneseen_us
dc.contributor.authorC., Roncolinien_us
dc.contributor.authorS., Silvestrien_us
dc.date.accessioned2021-03-30T14:36:04Z-
dc.date.available2021-03-30T14:36:04Z-
dc.date.issued1991-
dc.identifier.issn0006-3525en_US
dc.identifier.urihttp://hdl.handle.net/20.500.12779/3852-
dc.description55684en_US
dc.description.abstractBiotin–avidin recognition is studied by Fourier transform ir spectroscopy/attenuated total reflection (FTIR/ATR) under physiological conditions. The ureido portion of biotin is confirmed to be involved in the interaction with avidin, as previously found, but when the biotin–avidin complex forms, an electrostatic interaction occurs between the carboxylate group of the biotin molecule and the protonated aminic end group of the avidin amino acid side chains. Comparison of the biotin–avidin system with the biotin–1, 4-diaminobutane and biotin–tryptophan systems confirms these findings.en_US
dc.language.isoenen_US
dc.relationNoneen_US
dc.relation.ispartofBIOPOLYMERSen_US
dc.titleAntigen-Antibody recognition by Fourier Transform Infrared Spectroscopy (Attenuated Total Reflection) studies: Biotin-Avidin complex as an exampleen_US
dc.typeArticleen_US
dc.identifier.scopus2-s2.0-0026172009en_US
dc.relation.volume31en_US
dc.relation.issue7en_US
dc.description.firstpage827en_US
dc.description.lastpage834en_US
dc.description.thirdmissionNot applicableen_US
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeArticle-
item.fulltextNo Fulltext-
crisitem.author.orcid0000-0002-6960-9418-
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