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

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Title: Engineering Nanoparticle-Protein Associations for Protein Crystal Nucleation and Nanoparticle Arrangement
Author: Benoit, Denise
Advisor: Colvin, Vicki L.
Degree: Doctor of Philosophy thesis
Abstract: Engineering 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.
Citation: Benoit, Denise. (2012) "Engineering Nanoparticle-Protein Associations for Protein Crystal Nucleation and Nanoparticle Arrangement." Doctoral Thesis, Rice University. http://hdl.handle.net/1911/64716.
URI: http://hdl.handle.net/1911/64716
Date: 2012-09-05

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