dc.contributor.authorFan, Huien_US
dc.date.accessioned2008-09-17T11:42:03Z
dc.date.accessioned2017-07-23T08:42:07Z
dc.date.available2008-09-17T11:42:03Z
dc.date.available2017-07-23T08:42:07Z
dc.date.copyright2007en_US
dc.date.issued2007
dc.identifier.citationFan, H. (2007). Functional and structural studies of Coronavirus ribonucleocapsid assembly. Doctoral thesis, Nanyang Technological University, Singapore.
dc.identifier.urihttp://hdl.handle.net/10356/6573
dc.description.abstractOur research found that the Coronavirus infectious bronchitis virus (IBV) nucleocapsid (N) protein consists of two domains: N-terminal domain and C-terminal domain, which are connected by an arginine, serine, alanine rich linker. The N-terminal domain of the IBV N protein exhibits typical RNA-binding protein’s features, with a flexible hairpin loop rich in basic residues and a hydrophobic floor, providing a module for specific interaction with RNA. The C-terminal domain forms a tightly intertwined dimer with an intermolecular four-stranded central ?-sheet platform flanked by a helices. A possible nucleocapsid formation model was proposed that the C-terminal domain forms a helical nucleocapsid scaffold by dimerization and interdimer stacking. The N-terminal domain connects to the helical scaffold by arginine, serine, alanine rich linker and is mainly responsible for RNA binding.en_US
dc.rightsNanyang Technological Universityen_US
dc.subjectDRNTU::Science::Biological sciences::Microbiology::Virologyen_US
dc.titleFunctional and structural studies of Coronavirus ribonucleocapsid assemblyen_US
dc.typeThesisen_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.contributor.supervisorJulien Lescaren_US
dc.description.degreeDOCTOR OF PHILOSOPHY (SBS)en_US
dc.identifier.doihttps://doi.org/10.32657/10356/6573


Files in this item

FilesSizeFormatView
SBS-THESES_2.pdf6.505Mbapplication/pdfView/Open

This item appears in the following Collection(s)

Show simple item record