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An effort to experiment on the novel Usutu virus in pure in silico methods was made to determine conformational changes with non polar point mutations in the amino acid sequence. The first method consisted of creating a Python program to exhaustively identify codons, amino acids, and dinucleotide bridges & nonbridges, including viral characteristics defined by Mollentze in 2021. The second method consisted of creating point mutations to non polar amino acids in deemed key sites of the Usutu virus envelope protein and finding the RMSD from the original structure. This resulted in one of two outcomes - either the experiment showed that the Usutu virus envelope protein is highly resistant to point mutations or in silico methods are inconsistent and biased, leading to inaccuracy.
- Burton, Reilly (Author)
- Mills, Jeremy (Thesis director)
- Sterner, Beckett (Committee member)
- Upham, Nathan (Committee member)
- Barrett, The Honors College (Contributor)
- Division of Teacher Preparation (Contributor)
- School of Molecular Sciences (Contributor)
- 2023-05-05 11:43:13
- 2023-05-23 04:42:01
- 1 year 6 months ago