Structure - functional relationships of Right handed coiled-coil (RHCC) from the Archaea, Staphylothermus marinus

dc.contributor.authorOgbomo, Efehi Kelly
dc.contributor.examiningcommitteeCourt, Deborah (Microbiology) Wang, Feiyue (Chemistry)en
dc.contributor.supervisorStetefeld, Jörg (Chemistry)en
dc.date.accessioned2010-09-10T13:33:22Z
dc.date.available2010-09-10T13:33:22Z
dc.date.issued2010-09-10T13:33:22Z
dc.degree.disciplineChemistryen_US
dc.degree.levelMaster of Science (M.Sc.)en_US
dc.description.abstractHyperthermophilic 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.description.noteOctober 2010en
dc.format.extent1381914 bytes
dc.format.mimetypeapplication/pdf
dc.identifier.citationNo Citationen
dc.identifier.urihttp://hdl.handle.net/1993/4124
dc.language.isoengen_US
dc.rightsopen accessen_US
dc.subjectHyperthermophileen
dc.subjectCoiled coilen
dc.subjectS-layeren
dc.subjectMercuryen
dc.subjectHydrophobic cavityen
dc.subjectBioremediationen
dc.titleStructure - functional relationships of Right handed coiled-coil (RHCC) from the Archaea, Staphylothermus marinusen
dc.typemaster thesisen_US
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