Note: This work of creative scholarship is rooted in collaboration between three female artist-scholars: Carly Bates, Raji Ganesan, and Allyson Yoder. Working from a common intersectional, feminist framework, we served as artistic co-directors of each other’s solo pieces and co-producers of Negotiations, in which we share these pieces alongside each other. Negotiations is not a showcase of three individual works, but a conversation among three voices. As collaborators, we have been uncompromising in the pursuit of our own unique inquiries and voices and each of our works of creative scholarship stand alone. However, we believe that all of the parts are best understood in relationship to each other and to the whole. For this reason, we have chosen to cross-reference our thesis documents here, and we encourage readers to view the performance of Negotiations in its entirety.
Thesis documents cross-referenced:
French Vanilla: An Exploration of Biracial Identity Through Narrative Performance, by Carly Bates
Bhairavi: A Performance-Investigation of Belonging and Dis-Belonging in Diaspora Communities, by Raji Ganesan
Deep roots, shared fruits: Emergent creative process and the ecology of solo performance through “Dress in Something Plain and Dark,” by Allyson Yoder
Viral protein U (Vpu) is a type-III integral membrane protein encoded by Human Immunodeficiency Virus-1 (HIV- 1). It is expressed in infected host cells and plays several roles in viral progeny escape from infected cells, including down-regulation of CD4 receptors. But key structure/function questions remain regarding the mechanisms by which the Vpu protein contributes to HIV-1 pathogenesis. Here we describe expression of Vpu in bacteria, its purification and characterization. We report the successful expression of PelB-Vpu in Escherichia coli using the leader peptide pectate lyase B (PelB) from Erwinia carotovora. The protein was detergent extractable and could be isolated in a very pure form. We demonstrate that the PelB signal peptide successfully targets Vpu to the cell membranes and inserts it as a type I membrane protein. PelB-Vpu was biophysically characterized by circular dichroism and dynamic light scattering experiments and was shown to be an excellent candidate for elucidating structural models.