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Teague"]},{"label":"Rights Link","value":"<a href=\"https://rightsstatements.org/page/InC/1.0/?language=en\" target=\"_blank\"> In Copyright</a>"},{"label":"Rights","value":["In Copyright"]},{"label":"Decade","value":["2020s"]},{"label":"Type","value":["Text"]},{"label":"Holding Institution","value":["Berry College"]},{"label":"Extent","value":"12 pages"},{"label":"Medium","value":["theses"]},{"label":"Publisher","value":["Berry College"]},{"label":"Language (DLG)","value":["eng"]},{"label":"Language","value":["English"]},{"label":"Format","value":["application/pdf"]},{"label":"Description","value":"West Nile Virus is an arthropod-borne virus of the Flaviviridae family. The C-protein mediates binding to viral genomic RNA and membranes, and is essential in viral replication and proliferation. Homodimerization (Figure 1) is essential for functionality, and in previous studies, tryptophan 69 (W69) has been shown to be an important residue in dimerization. In this study, we investigate the effects on dimerization of a W69A mutation via crosslinking experiments and assembly assays. We found the mutation W69A partially inhibited dimerization and also required more RNA for assembly."},{"label":"Date","value":"April 30 2025"},{"label":"Date (Filter)","value":"D:30 M:04 Y:2025"},{"label":"Creator","value":["Victoria N. Teague"]},{"label":"Title","value":"Effect of W69A Mutation to the Capsid Protein of West Nile Virus on Dimerization and Viral Assembly"},{"label":"Faculty Advisor","value":["Savannah Post","Caitlin Conn"]},{"label":"Major","value":["Biochemistry"]}],"description":"Effect of W69A Mutation to the Capsid Protein of West Nile Virus on Dimerization and Viral 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