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dc.contributor.advisorKimberly Hamad-Schifferli.en_US
dc.contributor.authorRosenbaum, Lara Eliseen_US
dc.contributor.otherMassachusetts Institute of Technology. Dept. of Mechanical Engineering.en_US
dc.date.accessioned2008-02-27T22:29:08Z
dc.date.available2008-02-27T22:29:08Z
dc.date.copyright2007en_US
dc.date.issued2007en_US
dc.identifier.urihttp://hdl.handle.net/1721.1/40471
dc.descriptionThesis (S.B.)--Massachusetts Institute of Technology, Dept. of Mechanical Engineering, 2007.en_US
dc.descriptionIncludes bibliographical references (leaf 20).en_US
dc.description.abstractMaintaining protein function at the biological-inorganic interface is a critical challenge for bionanotechnology. Specifically, nanoparticle-protein conjugates must be designed to interact with binding partners with biologically-relevant thermodynamics. Towards developing a nanoparticle-tagging system that minimizes interference with normal protein function, here we design and begin development of an assay to assess complex formation between nanoparticle-immobilized proteins and soluble binding partners. Two chaperone proteins, importin-a and importin-3 mediate classical nuclear transport, an essential and highly conserved example of protein complex formation in eukaryotic cells. Together, these two proteins form a chaperone complex that recognizes a nuclear localization signal (NLS), which is a short peptide sequence. Here, we synthesize and purify a fluorescently-labeled importin-a and a positive control for complex formation, which consists of bovine albumin serum (BSA) covalently conjugated to a fluorophore and NLS. Using these two fluorescent molecules, we can perform Forster Resonance Energy Transfer (FRET) experiments to study the kinetics and thermodynamics of these protein interactions. The development of this system will be used in future tests with the NLS-conjugated fluorescent gold nanoparticles.en_US
dc.description.statementofresponsibilityby Lara Elise Rosenbaum.en_US
dc.format.extent24 leavesen_US
dc.language.isoengen_US
dc.publisherMassachusetts Institute of Technologyen_US
dc.rightsM.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.en_US
dc.rights.urihttp://dspace.mit.edu/handle/1721.1/7582
dc.subjectMechanical Engineering.en_US
dc.titleDesign of an in vitro assay to optimize assembly of nanoparticle-tagged nuclear import complexesen_US
dc.typeThesisen_US
dc.description.degreeS.B.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Dept. of Mechanical Engineering.en_US
dc.identifier.oclc191748948en_US


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