Nature of Mesoscopic Aggregates in Solutions of Lysozyme

Simple item page
dc.contributor.advisorWoehl, Taylor Jen_US
dc.contributor.advisorAnisimov, Mikhailen_US
dc.contributor.authorNIKFARJAM, SHAKIBAen_US
dc.contributor.departmentChemical Engineeringen_US
dc.contributor.publisherDigital Repository at the University of Marylanden_US
dc.contributor.publisherUniversity of Maryland (College Park, Md.)en_US
dc.date.accessioned2020-02-01T06:30:37Z
dc.date.available2020-02-01T06:30:37Z
dc.date.issued2018en_US
dc.description.abstractAn anomalous class of mesoscopic aggregates have previously been observed in solutions of lysozyme. These aggregates are thought to play an important role in nucleation of protein crystals and ordered protein aggregates, like amyloid fibers. Mesoscopic aggregates are currently thought to be in thermodynamic equilibrium with the protein solution, where transient oligomers of partially unfolded lysozyme monomers are thought to be the formation source of these aggregates. However, there is little experimental evidence to back up this proposed formation mechanism and thermodynamic behavior. Specifically, the effects of temperature on these aggregates and their thermodynamic reversibility have not been systematically tested. In this thesis, we investigate the equilibrium nature and the formation source of mesoscopic aggregates in solutions of model protein, lysozyme. We tested the effects of temperature on aggregate size and concentration and the aggregate reversibility after removal by systematic filtration. We used light and x-ray scattering and chromatography to experimentally characterize the aggregates during this study. Our findings indicate that mesoscopic aggregates are minimally sensitive to temperature changes and do not reform after removal by filtration. Together, these results indicate that mesoscopic aggregates are not in thermodynamic equilibrium with protein monomers or oligomers in solution. Overall, our experimental results contrast the current accepted formation mechanism of these mesoscopic aggregates and suggest they instead form due to contaminants present in solution or a sub-population of partially unfolded proteins.en_US
dc.identifierhttps://doi.org/10.13016/uevu-qejs
dc.identifier.urihttp://hdl.handle.net/1903/25354
dc.language.isoenen_US
dc.subject.pqcontrolledChemical engineeringen_US
dc.subject.pquncontrolledlysozymeen_US
dc.subject.pquncontrolledmesoscopicen_US
dc.subject.pquncontrolledProtein aggregationen_US
dc.subject.pquncontrolledreversibilityen_US
dc.titleNature of Mesoscopic Aggregates in Solutions of Lysozymeen_US
dc.typeThesisen_US

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
NIKFARJAM_umd_0117N_19984.pdf
Size:
1.45 MB
Format:
Adobe Portable Document Format
Download

Collections

UMD Theses and Dissertations
Chemical and Biomolecular Engineering Theses and Dissertations