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

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dc.contributor.advisor Young, Paul en
dc.contributor.author Murphy, Anita Catherine Honor
dc.date.accessioned 2016-11-25T10:21:07Z
dc.date.issued 2016
dc.date.submitted 2016
dc.identifier.citation Murphy, 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.endpage 290 en
dc.identifier.uri http://hdl.handle.net/10468/3314
dc.description.abstract Actinin 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.sponsorship Irish Research Council (EMBARK Postgraduate Research Scholarship Grant RS/2012/389) en
dc.format.mimetype application/pdf en
dc.language English en
dc.language.iso en en
dc.publisher University College Cork en
dc.rights © 2016, Anita Catherine Honor Murphy. en
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/3.0/ en
dc.subject Alpha-actinin en
dc.subject Actin en
dc.subject Congenital macrothrombocytopenia en
dc.subject Molecular self-assembly en
dc.subject Alpha-spectrin en
dc.subject Beta-spectrin en
dc.subject Actin-binding/bundling en
dc.subject Protein building blocks en
dc.subject Actinin-1 en
dc.title The actinin family of actin crosslinking proteins: natural functions and potential applications in synthetic biology en
dc.type Doctoral thesis en
dc.type.qualificationlevel Doctoral en
dc.type.qualificationname PhD (Science) en
dc.internal.availability Full text not available en
dc.check.info Restricted to everyone for three years en
dc.check.date 2019-11-25T10:21:07Z
dc.description.version Accepted Version
dc.contributor.funder Irish Research Council en
dc.description.status Not peer reviewed en
dc.internal.school Biochemistry en
dc.check.reason This thesis is due for publication or the author is actively seeking to publish this material en
dc.check.opt-out No en
dc.thesis.opt-out false
dc.check.entireThesis Entire Thesis Restricted
dc.check.embargoformat Both hard copy thesis and e-thesis en
ucc.workflow.supervisor p.young@ucc.ie
dc.internal.conferring Spring 2017 en


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© 2016, Anita Catherine Honor Murphy. Except where otherwise noted, this item's license is described as © 2016, Anita Catherine Honor Murphy.
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