dc.contributor.authorLim, Pei Yiing
dc.date.accessioned2016-10-28T08:03:26Z
dc.date.available2016-10-28T08:03:26Z
dc.date.issued2016-10-28
dc.identifier.urihttp://hdl.handle.net/10356/69099
dc.description.abstractNT5C2 relapse-associated mutations, K359Q and R367Q, are correlated with large gains in their enzymatic profiles. Crystal structures obtained in this study provide insights to the allosteric regulation mechanism of the enzyme by the disorder-to-order transition of a regulatory helix, which forms part of the active site. In addition, the mutant enzymes possess an increased basal level of activity and sensitivity to activation by effectors. In this study, the structural aspects of how each mutation potentially gains an advantage over the wild-type protein is revealed, with supporting evidence from biochemical and biophysical assays.en_US
dc.format.extent100 p.en_US
dc.language.isoenen_US
dc.subjectDRNTU::Scienceen_US
dc.titleStructural and functional studies of leukemia-associated mutations in human cytosolic 5'-nucleotidase IIen_US
dc.typeThesis
dc.contributor.supervisorPär Nordlunden_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.description.degreeMASTER OF SCIENCEen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record