The actinin family of actin crosslinking proteins: natural functions and potential applications in synthetic biology

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dc.check.embargoformatBoth hard copy thesis and e-thesisen
dc.check.opt-outNoen
dc.check.reasonThis thesis is due for publication or the author is actively seeking to publish this materialen
dc.contributor.advisorYoung, Paulen
dc.contributor.authorMurphy, Anita Catherine Honor
dc.contributor.funderIrish Research Councilen
dc.date.accessioned2016-11-25T10:21:07Z
dc.date.issued2016
dc.date.submitted2016
dc.description.abstractActinin and spectrin proteins are members of the Spectrin Family of Actin Crosslinking Proteins. The importance of these proteins in the cytoskeleton is demonstrated by the fact that they are common targets for disease causing mutations. In their most prominent roles, actinin and spectrin are responsible for stabilising and maintaining the muscle architecture during contraction, and providing shape and elasticity to the red blood cell in circulation, respectively. To carry out such roles, actinin and spectrin must possess important mechanical and physical properties. These attributes are desirable when choosing a building block for protein-based nanoconstruction. In this study, I assess the contribution of several disease-associated mutations in the actinin-1 actin binding domain that have recently been linked to a rare platelet disorder, congenital macrothrombocytopenia. I investigate the suitability of both actinin and spectrin proteins as potential building blocks for nanoscale structures, and I evaluate a fusion-based assembly strategy to bring about self-assembly of protein nanostructures. I report that the actinin-1 mutant proteins display increased actin binding compared to WT actinin-1 proteins. I find that both actinin and spectrin proteins exhibit enormous potential as nano-building blocks in terms of their stability and ability to self-assemble, and I successfully design and create homodimeric and heterodimeric bivalent building blocks using the fusion-based assembly strategy. Overall, this study has gathered helpful information that will contribute to furthering the advancement of actinin and spectrin knowledge in terms of their natural functions, and potential unnatural functions in protein nanotechnology.en
dc.description.sponsorshipIrish Research Council (EMBARK Postgraduate Research Scholarship Grant RS/2012/389)en
dc.description.statusNot peer revieweden
dc.description.versionAccepted Version
dc.format.mimetypeapplication/pdfen
dc.identifier.citationMurphy, A. C. H. 2016. The actinin family of actin crosslinking proteins: natural functions and potential applications in synthetic biology. PhD Thesis, University College Cork.en
dc.identifier.endpage290en
dc.identifier.urihttps://hdl.handle.net/10468/3314
dc.languageEnglishen
dc.language.isoenen
dc.publisherUniversity College Corken
dc.rights© 2016, Anita Catherine Honor Murphy.en
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/en
dc.subjectAlpha-actininen
dc.subjectActinen
dc.subjectCongenital macrothrombocytopeniaen
dc.subjectMolecular self-assemblyen
dc.subjectAlpha-spectrinen
dc.subjectBeta-spectrinen
dc.subjectActin-binding/bundlingen
dc.subjectProtein building blocksen
dc.subjectActinin-1en
dc.thesis.opt-outfalse
dc.titleThe actinin family of actin crosslinking proteins: natural functions and potential applications in synthetic biologyen
dc.typeDoctoral thesisen
dc.type.qualificationlevelDoctoralen
dc.type.qualificationnamePhD (Science)en
ucc.workflow.supervisorp.young@ucc.ie
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