<mods:mods xmlns:mods="http://www.loc.gov/mods/v3" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-7.xsd"><mods:titleInfo><mods:title>Forming Nanoparticle-Protein Conjugate Materials: Towards Fast Crystallization and Organized Assemblies</mods:title></mods:titleInfo><mods:typeOfResource authority="primo">dissertations</mods:typeOfResource><mods:name type="personal"><mods:namePart>Guo, Xiaoting</mods:namePart><mods:role><mods:roleTerm type="text">creator</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart>Colvin, Vicki</mods:namePart><mods:role><mods:roleTerm type="text">Advisor</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart>Sun, Shouheng</mods:namePart><mods:role><mods:roleTerm type="text">Reader</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart>Robinson, Jerome</mods:namePart><mods:role><mods:roleTerm type="text">Reader</mods:roleTerm></mods:role></mods:name><mods:name type="corporate"><mods:namePart>Brown University. Department of Chemistry</mods:namePart><mods:role><mods:roleTerm type="text">sponsor</mods:roleTerm></mods:role></mods:name><mods:originInfo><mods:copyrightDate>2023</mods:copyrightDate></mods:originInfo><mods:physicalDescription><mods:extent>22, 223 p.</mods:extent><mods:digitalOrigin>born digital</mods:digitalOrigin></mods:physicalDescription><mods:note type="thesis">Thesis (Ph. D.)--Brown University, 2023</mods:note><mods:genre authority="aat">theses</mods:genre><mods:abstract>Protein crystallization is essential for determining protein structures and understanding their functions. Recent studies have shown that protein crystal nucleation often involves a liquid-liquid phase separation (LLPS) that forms protein droplets, providing an opportunity to improve crystallization outcomes. In this study, we fabricated metal nanoparticle-polyethylene glycol (PEG) conjugates to promote protein crystal formation. By anchoring PEG to well-dispersed nanoparticles, we created a shell that potentially attracts protein molecules, increasing the chance of forming a critical nucleus. Our preliminary data show that these nanoparticle-polymer conjugates significantly enhance protein crystal formation by increasing crystal counts and reducing nucleation times. The effectiveness of this method is determined by the length of the PEG chains, with longer chains exhibiting stronger interactions with proteins. We demonstrated the utility of this approach using multiple protein species including hen egg white lysozyme (HEWL), revealing that the addition of gold nanoparticle-PEG conjugates increased the number of crystal hits and chances of acquiring perfect crystal forms, without sacrificing resolution under X-ray diffraction. Furthermore, nanoparticle-incorporated crystals can serve as composite materials to accommodate the 3D assembly of magnetic nanoparticles and quantum dots.</mods:abstract><mods:subject><mods:topic>Protein crystallization</mods:topic></mods:subject><mods:subject><mods:topic>nanoparticle conjugates</mods:topic></mods:subject><mods:language><mods:languageTerm authority="iso639-2b">English</mods:languageTerm></mods:language><mods:recordInfo><mods:recordContentSource authority="marcorg">RPB</mods:recordContentSource><mods:recordCreationDate encoding="iso8601">20230602</mods:recordCreationDate></mods:recordInfo></mods:mods>