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...

Full description

Saved in:
Bibliographic Details
Main Author: Gan, Siok Wan
Other Authors: Jaume Torres
Format: Theses and Dissertations
Language:English
Published: 2011
Subjects:
Online Access:https://hdl.handle.net/10356/42676
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Nanyang Technological University
Language: English
id sg-ntu-dr.10356-42676
record_format dspace
spelling sg-ntu-dr.10356-426762023-02-28T18:42:04Z Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein Gan, Siok Wan Jaume Torres School of Biological Sciences DRNTU::Science::Biological sciences::Microbiology::Virology 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. DOCTOR OF PHILOSOPHY (SBS) 2011-01-07T01:15:32Z 2011-01-07T01:15:32Z 2010 2010 Thesis Gan, S. W. (2010). Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein. Doctoral thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/42676 10.32657/10356/42676 en 141 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science::Biological sciences::Microbiology::Virology
spellingShingle DRNTU::Science::Biological sciences::Microbiology::Virology
Gan, Siok Wan
Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein
description 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.
author2 Jaume Torres
author_facet Jaume Torres
Gan, Siok Wan
format Theses and Dissertations
author Gan, Siok Wan
author_sort Gan, Siok Wan
title Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein
title_short Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein
title_full Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein
title_fullStr Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein
title_full_unstemmed Structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein
title_sort structural and functional characterization of the human respiratory syncytial virus small hydrophobic protein
publishDate 2011
url https://hdl.handle.net/10356/42676
_version_ 1759855893764112384