Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein
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. I...
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| Format: | Thesis |
| Sprog: | English |
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2011
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| Online adgang: | https://hdl.handle.net/10356/42676 |
| Summary: | 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. |
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