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dc.contributor.authorOberc, Christopher
dc.date.accessioned2015-07-07T17:50:22Z
dc.date.available2015-07-07T17:50:22Z
dc.identifier.urihttp://hdl.handle.net/10464/6927
dc.description.abstractThe opioid receptors consist of three main subtypes; μ, δ, and κ. Previous binding studies have shown that fragments of the milk protein, β-casein, known as β-casomorphins are agonists of these receptors which are selective for the μ receptor subtype. Using the crystal structures of these three receptors, computational molecular docking studies were done using the software GOLD to determine the conformation of β-casomorphin-5 and 7 when they bind to these three opioid receptors. GOLD was able to discriminate among the three receptors when docking the rigid ligands co-crystalized with the receptors. However, GOLD could not discriminate among the three receptors for either of the highly flexible β-casomorphins. A per amino acid scoring method was developed to overcome this problem. This method was used to predict the conformation of both β-casomorphin-5 and 7 in the μ receptor and determine that the two amino acid residues, Lys303 and Trp318 of the μ receptor are responsible for discriminating among the three receptor subtypes for binding of the β-casomorphin-5 and 7.en_US
dc.language.isoengen_US
dc.publisherBrock Universityen_US
dc.subjectOpioid Receptorsen_US
dc.subjectβ-Casomorphinsen_US
dc.subjectComputational Dockingen_US
dc.subjectPoseen_US
dc.titlePredicting the Pose of β-Casomorphin-5 and 7 in the Opioid Receptorsen_US
dc.typeElectronic Thesis or Dissertationen
dc.degree.nameM.Sc. Chemistryen_US
dc.degree.levelMastersen_US
dc.contributor.departmentDepartment of Chemistryen_US
dc.degree.disciplineFaculty of Mathematics and Scienceen_US
refterms.dateFOA2021-07-16T12:29:52Z


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