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dc.contributor.advisorMagliery, Thomas J.
dc.creatorThomas, Miriam
dc.descriptionCollege of Math and Physical Science Research Forum Award for Best Poster Presentation in Department of Chemistryen_US
dc.description.abstractMost natural proteins are only marginally stable, yet many therapeutic and industrial applications require stabilized variants. It has been shown that mutations to the most common residue in a multiple sequence alignment of protein families results in stabilization about half the time. The degree of conservation of these residues can be determined by measuring the difference between the amino acid distribution at a particular site and its neutral reference state. In this project, we examine if the degree of conservation for a position is related to its ability to affect the stability of the protein. Here, we are interested in studying the additive effects of mutating six positions in yeast triosephosphate isomerase (TIM) to consensus residues. To dissect the effects of these mutations, we are also constructing the six individual mutants which contain one highly conserved residue each. These variants will be studied for both structure and function. With this knowledge we will be able to reliably design more stable and functional proteins from genomic sequence data. This will have numerous benefits for research and industrial purposes, and will have potential health benefits in designing therapeutic proteins.en_US
dc.description.sponsorship2007 University Honors & Scholars Summer Research Intern Scholarshipen_US
dc.publisherThe Ohio State Universityen_US
dc.relation.ispartofseriesThe Ohio State University. Department of Chemistry Honors Theses; 2008en_US
dc.subjectprotein engineeringen_US
dc.subjectprotein stabilityen_US
dc.titleThe Effects of Consensus Mutations on Triosephosphate Isomeraseen_US
dc.description.embargoA one-year embargo was granted for this item.en_US
dc.rights.ccAttribution-NonCommercial-NoDerivs 3.0 Unporteden_US

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