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dc.contributor.advisorKlauda, Jeffery Ben_US
dc.contributor.authorRogaski, Brent Josephen_US
dc.date.accessioned2011-02-19T07:09:25Z
dc.date.available2011-02-19T07:09:25Z
dc.date.issued2010en_US
dc.identifier.urihttp://hdl.handle.net/1903/11239
dc.description.abstractOsh4 is an oxysterol binding protein homologue found in yeast that is essential for the intracellular transport of sterols. It has been proposed that Osh4 acts as a lipid transport protein, binding a single sterol residue and transporting it from the endoplasmic reticulum to the plasma membrane. The dynamics of Osh4 as well as ergosterol binding was observed using molecular dynamics simulations. Blind docking of several model lipid head group moieties was used to detect potential binding regions along the Osh4 surface favorable towards phospholipid interaction. Models frequently docked to a lysine-rich region on the side of the protein's β-barrel. A model ergosterol-containing membrane system for yeast was also constructed and simulated using molecular dynamics, and an improvement to the deuterium order parameters was observed over previous models. Understanding how Osh4 attaches to cellular membranes will lead to a clear understanding of how this protein transports sterols in vivo.en_US
dc.titleCOMPUTATIONAL STUDIES ON THE BINDING AND DYNAMICS OF THE OSH4 PROTEIN OF YEAST AND A MODEL YEAST MEMBRANE SYSTEMen_US
dc.typeThesisen_US
dc.contributor.publisherDigital Repository at the University of Marylanden_US
dc.contributor.publisherUniversity of Maryland (College Park, Md.)en_US
dc.contributor.departmentChemical Engineeringen_US
dc.subject.pqcontrolledBiophysicsen_US
dc.subject.pqcontrolledChemical Engineeringen_US
dc.subject.pquncontrolleddockingen_US
dc.subject.pquncontrolledmolecular dynamicsen_US
dc.subject.pquncontrolledOsh4en_US
dc.subject.pquncontrolledyeasten_US


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