Intermolecular forces at play in the active site of lactoperoxidase

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dc.contributor.advisorLlano, Jorge
dc.contributor.authorManary, Brandon
dc.date.accessioned2016-05-27
dc.date.accessioned2022-05-28T00:38:29Z
dc.date.available2022-05-28T00:38:29Z
dc.date.issued2016
dc.descriptionPresented on January 25, 2016 at Student Research Week held at MacEwan University in Edmonton, Alberta.
dc.description.abstractLactoperoxidase (LPO) is an enzyme that fights in the first line of defense against infection. LPO catalyzes the formation of toxic chemicals which indiscriminately kill foreign microbes and viruses caught in the mucous membranes of vulnerable body parts (namely, the eyes and upper airways). Because of its importance for the immune system, LPO is largely studied for potential applications in medical therapies. However, while much research has been done to determine the protein's structure and its efficacy against various pathogens, the chemical mechanism by which the enzyme's active-site transforms common ions into germ-killing agents is not known in detail. The aim of this project is to apply methods of computational chemistry and bioinformatics implemented in state-of-the-art software to elucidate the catalytic mechanism of LPO with common substrates found in the body fluids.
dc.format.extent1.61 MB
dc.format.mimetypePDF
dc.identifier.urihttps://hdl.handle.net/20.500.14078/1041
dc.languageEnglish
dc.language.isoen
dc.rightsAll Rights Reserved
dc.subjectlactoperoxidase
dc.subjectimmune system
dc.titleIntermolecular forces at play in the active site of lactoperoxidase
dc.typeStudent Presentation
dspace.entity.type
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