Intersections of Gay and Bisexual Identity with Fatness

This thesis examines the intersections of gay and bisexual identity with body size, or fatness. Gay and bisexual identity and fatness are marginalized social identities that seem to be incompatible (Bond, 2013). While a sense of collective identity with the gay and bisexual community has been shown to be a protective factor against internalized homonegativity in gay and bisexual men (Halpin & Allen, 2004), the degree to which this protective factor persists for fat people in an anti-fat environment like the gay and bisexual community (Wrench & Knapp, 2008) has not been explored. This intersection of identities and anti-fat culture seemed to suggest there might be a relationship between fatness and internalized homophobia. Fatness did not moderate the relationship between sense of belonging to the gay and bisexual community and internalized homonegativity, but a significant positive relationship was found between belongingness to the gay and bisexual community and body shame.

STRUCTURAL AND FUNCTIONAL STUDIES OF CYCLIC K48-LINKED DIUBIQUITIN

K48-linked di-ubiquitin exists in a dynamic equilibrium between open and closed states. The structure of K48-Ub2 in the closed conformation features a hydrophobic interface formed between the two Ub domains. The same hydrophobic residues at the interface are involved in binding to ubiquitin-associated (UBA) domains. Cyclization of K48-Ub2 should limit the range of conformations available for such interactions. Interestingly, cyclic K48-linked Ub2 (cycUb2) has been found in vivo and can be isolated in vitro to study its structure and dynamics. In this study, a crystal structure of cycUb2 was obtained, and the dynamics of cycUb2 were characterized by solution NMR. The crystal structure of cycUb2, which is in agreement with solution NMR data, is closed with the hydrophobic patches of each Ub domain buried at the interface. Despite its structural constraints, cycUb2 was still able to interact with UBA domains, albeit with lower affinity.