Identifying the role of cysteine residues in SARS coronavirus envelope (E) protein oligomerization by using analytical ultracentrifugation and SDS-PAGE.
Coronaviruses had caused a pandemic disease, severe acute respiratory syndrome (SARS) around the world in 2003. The viral membrane proteins always become extremely crucial molecules in viral assembly and viral replication. In SARS-Coronavirus, its membrane consists of at least membrane (M), spike (S...
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| Format: | Final Year Project (FYP) |
| Language: | English |
| Published: |
2010
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| Online Access: | http://hdl.handle.net/10356/39914 |
| _version_ | 1826116366854258688 |
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| author | Go, Ka Diam. |
| author2 | Jaume Torres |
| author_facet | Jaume Torres Go, Ka Diam. |
| author_sort | Go, Ka Diam. |
| collection | NTU |
| description | Coronaviruses had caused a pandemic disease, severe acute respiratory syndrome (SARS) around the world in 2003. The viral membrane proteins always become extremely crucial molecules in viral assembly and viral replication. In SARS-Coronavirus, its membrane consists of at least membrane (M), spike (S), and envelope (E) proteins. From those proteins, E protein function is still unknown. Other study has showed palmitoylations of cysteine residues in E protein are crucial for protein stability as well as for viral assembly. Meanwhile, in another study of our lab, it was shown that SARS-CoV E proteins formed homopentameric model when it was run in PFO-PAGE. Thus, in this project, it is suggested that cysteine residues in E protein might form disulfide linkages to improve the stability of that pentameric model. By using analytical ultracentrifugation method and SDS-PAGE, we were trying to find out the role of cysteine residues in single, double, and triple-substitution of E protein mutants. The results showed that disulfide bond was not the primary factor in the pentameric formation of SARS-CoV E protein. Further investigation has showed that E proteins were aggregated before they were analyzed in analytical ultracentrifugation sedimentation equilibrium. Thus, to avoid aggregation, future studies needs to use lower protein concentration or higher detergent concentration. |
| first_indexed | 2024-10-01T04:10:32Z |
| format | Final Year Project (FYP) |
| id | ntu-10356/39914 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T04:10:32Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | ntu-10356/399142023-02-28T18:06:46Z Identifying the role of cysteine residues in SARS coronavirus envelope (E) protein oligomerization by using analytical ultracentrifugation and SDS-PAGE. Go, Ka Diam. Jaume Torres School of Biological Sciences BioSciences Research Centre DRNTU::Science::Biological sciences::Microbiology::Virology Coronaviruses had caused a pandemic disease, severe acute respiratory syndrome (SARS) around the world in 2003. The viral membrane proteins always become extremely crucial molecules in viral assembly and viral replication. In SARS-Coronavirus, its membrane consists of at least membrane (M), spike (S), and envelope (E) proteins. From those proteins, E protein function is still unknown. Other study has showed palmitoylations of cysteine residues in E protein are crucial for protein stability as well as for viral assembly. Meanwhile, in another study of our lab, it was shown that SARS-CoV E proteins formed homopentameric model when it was run in PFO-PAGE. Thus, in this project, it is suggested that cysteine residues in E protein might form disulfide linkages to improve the stability of that pentameric model. By using analytical ultracentrifugation method and SDS-PAGE, we were trying to find out the role of cysteine residues in single, double, and triple-substitution of E protein mutants. The results showed that disulfide bond was not the primary factor in the pentameric formation of SARS-CoV E protein. Further investigation has showed that E proteins were aggregated before they were analyzed in analytical ultracentrifugation sedimentation equilibrium. Thus, to avoid aggregation, future studies needs to use lower protein concentration or higher detergent concentration. Bachelor of Science in Biological Sciences 2010-06-08T01:55:15Z 2010-06-08T01:55:15Z 2010 2010 Final Year Project (FYP) http://hdl.handle.net/10356/39914 en Nanyang Technological University 47 p. application/pdf |
| spellingShingle | DRNTU::Science::Biological sciences::Microbiology::Virology Go, Ka Diam. Identifying the role of cysteine residues in SARS coronavirus envelope (E) protein oligomerization by using analytical ultracentrifugation and SDS-PAGE. |
| title | Identifying the role of cysteine residues in SARS coronavirus envelope (E) protein oligomerization by using analytical ultracentrifugation and SDS-PAGE. |
| title_full | Identifying the role of cysteine residues in SARS coronavirus envelope (E) protein oligomerization by using analytical ultracentrifugation and SDS-PAGE. |
| title_fullStr | Identifying the role of cysteine residues in SARS coronavirus envelope (E) protein oligomerization by using analytical ultracentrifugation and SDS-PAGE. |
| title_full_unstemmed | Identifying the role of cysteine residues in SARS coronavirus envelope (E) protein oligomerization by using analytical ultracentrifugation and SDS-PAGE. |
| title_short | Identifying the role of cysteine residues in SARS coronavirus envelope (E) protein oligomerization by using analytical ultracentrifugation and SDS-PAGE. |
| title_sort | identifying the role of cysteine residues in sars coronavirus envelope e protein oligomerization by using analytical ultracentrifugation and sds page |
| topic | DRNTU::Science::Biological sciences::Microbiology::Virology |
| url | http://hdl.handle.net/10356/39914 |
| work_keys_str_mv | AT gokadiam identifyingtheroleofcysteineresiduesinsarscoronavirusenvelopeeproteinoligomerizationbyusinganalyticalultracentrifugationandsdspage |