dc.contributor.authorKang, Congbaoen_US
dc.date.accessioned2008-09-17T11:42:14Z
dc.date.accessioned2017-07-23T08:42:08Z
dc.date.available2008-09-17T11:42:14Z
dc.date.available2017-07-23T08:42:08Z
dc.date.copyright2006en_US
dc.date.issued2006
dc.identifier.citationKang, C. B. (2006). Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2. Doctoral thesis, Nanyang Technological University, Singapore.
dc.identifier.urihttp://hdl.handle.net/10356/6582
dc.description.abstractFK506 binding protein (FKBP) 38, which is a tripartite TPR domain-containing member in the FKBP family, can help Bcl-2 localize at the mitochondrial membrane and modulate apoptosis. The regulation of Bcl-2 function by forming heterodimeric complexes with its pro-apoptotic partners is well studied. Bcl-2 is also regulated at the posttranslational level through phosphorylation of specific residues within the flexible loop. Bcl-2 contains an unusually long loop between the first and the second helices. This loop has been shown to be highly flexible based on NMR and X-ray crystallographic analyses of this region. Currently, the molecular basis of alternative regulatory mechanism of Bcl-2 remains poorly understood.en_US
dc.rightsNanyang Technological Universityen_US
dc.subjectDRNTU::Science::Biological sciences::Molecular biologyen_US
dc.titleBiochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2en_US
dc.typeThesisen_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.contributor.supervisorYoon, Ho Supen_US
dc.description.degreeDOCTOR OF PHILOSOPHY (SBS)en_US


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