Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/42676
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dc.contributor.authorGan, Siok Wanen
dc.date.accessioned2011-01-07T01:15:32Zen
dc.date.available2011-01-07T01:15:32Zen
dc.date.copyright2010en
dc.date.issued2010en
dc.identifier.citationGan, S. W. (2010). Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein. Doctoral thesis, Nanyang Technological University, Singapore.en
dc.identifier.urihttps://hdl.handle.net/10356/42676en
dc.description.abstractThe small hydrophobic (SH) protein is a transmembrane surface glycoprotein encoded by the respiratory syncytial virus (RSV). It is 64 amino acids long with one putative transmembrane domain. Although SH protein is important for viral infectivity, its exact role during viral infection is not clear. In this study, we have examined the structure, oligomerization, and function of SH protein and the transmembrane domain (SH-TM) using biochemical, biophysical and computational approaches.en
dc.format.extent141 p.en
dc.language.isoenen
dc.subjectDRNTU::Science::Biological sciences::Microbiology::Virologyen
dc.titleStructural and functional characterization of the human respiratory syncytial virus small hydrophobic proteinen
dc.typeThesisen
dc.contributor.supervisorJaume Torresen
dc.contributor.schoolSchool of Biological Sciencesen
dc.description.degreeDOCTOR OF PHILOSOPHY (SBS)en
dc.identifier.doi10.32657/10356/42676en
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