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dc.contributor.supervisor Stetefeld, Jörg (Chemistry) en
dc.contributor.author Ogbomo, Efehi Kelly
dc.date.accessioned 2010-09-10T13:33:22Z
dc.date.available 2010-09-10T13:33:22Z
dc.date.issued 2010-09-10T13:33:22Z
dc.identifier.citation No Citation en
dc.identifier.uri http://hdl.handle.net/1993/4124
dc.description.abstract Hyperthermophilic proteins are of great interest in both the academic and industrial world in understanding how these proteins are capable of retaining their biological activity under such harsh environmental conditions. This thesis studies a tetrabrachion stalk domain from Staphylothermus marinus, know as Right Handed Coiled Coil (RHCC). This protein is of interest due to its extreme thermostability and its affinity for heavy metals. We aim to better understand the reason for the extreme thermal stability of the protein and to take advantage of the proteins affinity for heavy metals with a view to developing a novel approach to bioremediate Hg2+, a major environmental pollutant. Our results clearly indicated that the protein is more thermostable in alkaline conditions in comparison to acidic conditions. This observation can be explained by careful inspection of the high resolution structure. Our data also clearly show that RHCC is able to bind ionic mercury compounds such as mercury nitrate and dipotassium mercury iodide. en
dc.format.extent 1381914 bytes
dc.format.mimetype application/pdf
dc.language.iso en_US
dc.rights info:eu-repo/semantics/openAccess
dc.subject Hyperthermophile en
dc.subject Coiled coil en
dc.subject S-layer en
dc.subject Mercury en
dc.subject Hydrophobic cavity en
dc.subject Bioremediation en
dc.title Structure - functional relationships of Right handed coiled-coil (RHCC) from the Archaea, Staphylothermus marinus en
dc.type info:eu-repo/semantics/masterThesis
dc.degree.discipline Chemistry en
dc.contributor.examiningcommittee Court, Deborah (Microbiology) Wang, Feiyue (Chemistry) en
dc.degree.level Master of Science (M.Sc.) en
dc.description.note October 2010 en


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