Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/42676
Title: Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein
Authors: Gan, Siok Wan
Keywords: DRNTU::Science::Biological sciences::Microbiology::Virology
Issue Date: 2010
Source: Gan, S. W. (2010). Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein. Doctoral thesis, Nanyang Technological University, Singapore.
Abstract: The 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.
URI: https://hdl.handle.net/10356/42676
DOI: 10.32657/10356/42676
Schools: School of Biological Sciences 
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Theses

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