Engineering streptavidin and its target ligands with both infinite binding affinity and reversible binding capability

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atmire.migration.oldid2997
dc.contributor.advisorWong, Sui-Lam
dc.contributor.authorFogen, Dawson
dc.date.accessioned2015-02-06T18:52:28Z
dc.date.available2015-06-23T07:00:45Z
dc.date.issued2015-02-06
dc.date.submitted2015en
dc.description.abstractFor development of reusable biosensor chips, bioreactors, protein arrays, and matrices for affinity purification of proteins, it would be ideal for streptavidin to have extremely tight binding to its target ligands (biotin and its binding tags) and at the same time to retain the feature of reversible binding capability. To achieve this objective, a streptavidin mutein (SAVSBPM32) was engineered based on a previously engineered streptavidin variant (SAVSBPM18) that can bind both biotin and its binding tag in a reversible manner. Cysteine residues were placed in strategic positions in both the streptavidin mutein and its binding tags. Disulfide bond formation allows immobilization of tagged proteins to streptavidin. Incubation with biotin in the presence of reducing agents allows stripping off tagged proteins from streptavidin.en_US
dc.identifier.citationFogen, D. (2015). Engineering streptavidin and its target ligands with both infinite binding affinity and reversible binding capability (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/25896en_US
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/25896
dc.identifier.urihttp://hdl.handle.net/11023/2088
dc.language.isoeng
dc.publisher.facultyGraduate Studies
dc.publisher.institutionUniversity of Calgaryen
dc.publisher.placeCalgaryen
dc.rightsUniversity of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.
dc.subjectBiology
dc.subjectMicrobiology
dc.subjectBiology--Molecular
dc.subject.classificationStreptavidinen_US
dc.subject.classificationStreptavidin Binding Peptideen_US
dc.subject.classificationPeptide Tag for Biotinylationen_US
dc.titleEngineering streptavidin and its target ligands with both infinite binding affinity and reversible binding capability
dc.typemaster thesis
thesis.degree.disciplineBiological Sciences
thesis.degree.grantorUniversity of Calgary
thesis.degree.nameMaster of Science (MSc)
ucalgary.item.requestcopytrue
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