Computational assessment of structural stability of E protein variants in coronaviridae
Studies on coronaviruses have received spotlight due to the CoVID-19 pandemic. These studies range from determining the structure of the protein, pathway of infection to exploring therapeutic targets within the protein. Although E protein has been proven critical for viral assembly and maturati...
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| 格式: | Final Year Project |
| 語言: | English |
| 出版: |
Nanyang Technological University
2022
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| 主題: | |
| 在線閱讀: | https://hdl.handle.net/10356/160699 |
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| 機構: | Nanyang Technological University |
| 語言: | English |
| 總結: | Studies on coronaviruses have received spotlight due to the CoVID-19 pandemic. These studies
range from determining the structure of the protein, pathway of infection to exploring therapeutic
targets within the protein. Although E protein has been proven critical for viral assembly and
maturation and is completely conserved in genomes of all four genera of the coronaviridae, little
is known about the function of the smallest protein encoded in SARS-CoV-2. There are many
uncertainties regarding reliability of Swiss Model predicting its 3D structure though it is the most
used homology modelling server. In this study, Molecular Dynamics simulation was performed
for 1 sequence per genus to check their stability in a lipid bilayer using GROMACS. The
primary focus is to identify the most thermostable sequence variant of E protein with the greatest
potential for structural and drug discovery studies. Results showed that the sequence from Delta
genera was the most stable, followed by Beta, Alpha then Gamma. Although conclusion derived
from Swiss Model and simulations were the same, the simulations were more informative and
reliable. Findings presented provide an alternative to traditional homology modelling and
provide a deeper understanding to E proteins stability and their amenability to structural and
relationship studies. |
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