Engineering Nanoparticle-Protein Associations for Protein Crystal Nucleation and Nanoparticle Arrangement

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dc.contributor.advisorColvin, Vicki L.en_US
dc.contributor.committeeMemberShamoo, Yousifen_US
dc.contributor.committeeMemberHartgerink, Jeffrey D.en_US
dc.creatorBenoit, Deniseen_US
dc.date.accessioned2012-09-06T04:48:48Zen_US
dc.date.accessioned2012-09-06T04:48:55Zen_US
dc.date.available2012-09-06T04:48:48Zen_US
dc.date.available2012-09-06T04:48:55Zen_US
dc.date.created2012-05en_US
dc.date.issued2012-09-05en_US
dc.date.submittedMay 2012en_US
dc.date.updated2012-09-06T04:48:55Zen_US
dc.description.abstractEngineering the nanoparticle - protein association offers a new way to form protein crystals as well as new approaches for arrangement of nanoparticles. Central to this control is the nanoparticle surface. By conjugating polymers on the surface with controlled molecular weights many properties of the nanoparticle can be changed including its size, stability in buffers and the association of proteins with its surface. Large molecular weight poly(ethylene glycol) (PEG) coatings allow for weak associations between proteins and nanoparticles. These interactions can lead to changes in how proteins crystallize. In particular, they decrease the time to nucleation and expand the range of conditions over which protein crystals form. Interestingly, when PEG chain lengths are too short then protein association is minimized and these effects are not observed. One important feature of protein crystals nucleated with nanoparticles is that the nanoparticles are incorporated into the crystals. What results are nanoparticles placed at well-defined distances in composite protein-nanoparticle crystals. Crystals on the size scale of 10 - 100 micrometers exhibit optical absorbance, fluorescence and super paramagnetic behavior derivative from the incorporated nanomaterials. The arrangement of nanoparticles into three dimensional arrays also gives rise to new and interesting physical and chemical properties, such as fluorescence enhancement and varied magnetic response. In addition, anisotropic nanomaterials aligned throughout the composite crystal have polarization dependent optical properties.en_US
dc.format.mimetypeapplication/pdfen_US
dc.identifier.citationBenoit, Denise. "Engineering Nanoparticle-Protein Associations for Protein Crystal Nucleation and Nanoparticle Arrangement." (2012) Diss., Rice University. <a href="https://hdl.handle.net/1911/64716">https://hdl.handle.net/1911/64716</a>.en_US
dc.identifier.slug123456789/ETD-2012-05-196en_US
dc.identifier.urihttps://hdl.handle.net/1911/64716en_US
dc.language.isoengen_US
dc.rightsCopyright is held by the author, unless otherwise indicated. Permission to reuse, publish, or reproduce the work beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.en_US
dc.subjectNanoparticlesen_US
dc.subjectNanoparticle-protein associationen_US
dc.subjectNanoparticle arrangementen_US
dc.subjectProtein crystallographyen_US
dc.titleEngineering Nanoparticle-Protein Associations for Protein Crystal Nucleation and Nanoparticle Arrangementen_US
dc.typeThesisen_US
dc.type.materialTexten_US
thesis.degree.departmentChemistryen_US
thesis.degree.disciplineNatural Sciencesen_US
thesis.degree.grantorRice Universityen_US
thesis.degree.levelDoctoralen_US
thesis.degree.nameDoctor of Philosophyen_US
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