Crystallographic and Biochemical Studies of a Streptavidin Mutant: the Structural Basis of Ligand Recognition and Conformational Changes

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atmire.migration.oldid4764
dc.contributor.advisorNg, Kenneth
dc.contributor.authorArellano Saab, Amir Alam
dc.contributor.committeememberWong, Sui-Lam
dc.contributor.committeememberMoorhead, Gregory
dc.date.accessioned2016-08-19T17:12:59Z
dc.date.available2016-08-19T17:12:59Z
dc.date.issued2016
dc.date.submitted2016en
dc.description.abstractA variant of streptavidin, SAVSBPM32, was previously designed to incorporate mutations that weaken binding to biotin and introduce a cysteine at position 86. Streptavidin-binding peptides have also been re-designed to test the binding capabilities of SAVSBPM32. The primary goal of this project was to crystallize SAVSBPM32 and evaluate its interactions with biotin, a cysteine containing SBP-Tag and a cysteine containing a biotinylation tag (CPFB-2). The crystal structure of SAVSBPM32 in complex with biotin revealed for the first time that the loop bridging the third and fourth b-strands in SAVSBPM32 can adopt a closed or an open conformation. The crystal structure of SAVSBPM32 in complex with CPFB-2 reveals the novel structure of a biotinylated peptide bound to streptavidin while also forming a disulphide bond. These findings confirm key design principles and suggest approaches for further development.en_US
dc.identifier.citationArellano Saab, A. A. (2016). Crystallographic and Biochemical Studies of a Streptavidin Mutant: the Structural Basis of Ligand Recognition and Conformational Changes (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/25498en_US
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/25498
dc.identifier.urihttp://hdl.handle.net/11023/3192
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.subjectBiology--Molecular
dc.subjectBiochemistry
dc.subject.classificationStreptavidinen_US
dc.subject.classificationCrystallographyen_US
dc.subject.classificationBiochemistryen_US
dc.subject.classificationMutationen_US
dc.subject.classificationStructureen_US
dc.titleCrystallographic and Biochemical Studies of a Streptavidin Mutant: the Structural Basis of Ligand Recognition and Conformational Changes
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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