Creation of a Site-Directed Mutant of Hen Egg White Lysozyme Working Toward Site-Specific Oxidation as it Relates to Protein Structure

Mensah, Eric

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dc.contributor.author	Mensah, Eric	en_US
dc.date.accessioned	2013-12-04T16:03:30Z
dc.date.accessioned	2019-09-08T02:37:35Z
dc.date.available	2013-12-04T16:03:30Z
dc.date.available	2019-09-08T02:37:35Z
dc.date.issued	2009
dc.identifier	459787180	en_US
dc.identifier.other	b20530286	en_US
dc.identifier.uri	http://hdl.handle.net/1989/10726
dc.description	xiii, 64 leaves : ill. ; 29 cm.	en_US
dc.description.abstract	Metal catalyzed oxidation of protein involves a reaction between hydrogen peroxide and protein-bound metal ions. Production of the highly-reactive hydroxyl radical leads to oxidative damage in the immediate vicinity of the bound-metal ion. To examine the relationship between protein structure and oxidative damage a series of site-directed mutants of hen egg white lysozyme (HEWL) were created. This project focuses on generation of the site directed mutant where residue His15 will be altered to a serinyl residue (H15S), also work on the preliminary purification and characterization of the putative mutant would be touched on.	en_US
dc.description.statementofresponsibility	by Eric Mensah.	en_US
dc.language.iso	en_US	en_US
dc.relation.ispartofseries	Master's Theses no. 1151	en_US
dc.subject.lcsh	Lysozyme.	en_US
dc.subject.lcsh	Oxidation.	en_US
dc.subject.lcsh	Proteins--Structure.	en_US
dc.subject.lcsh	Active oxygen.	en_US
dc.title	Creation of a Site-Directed Mutant of Hen Egg White Lysozyme Working Toward Site-Specific Oxidation as it Relates to Protein Structure	en_US
dc.type	Thesis	en_US

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