Location
Northwestern College, Rowenhorst Student Center
Abstract
Examining protein-protein interactions in vivo can often be challenging due to nonspecific cross reactivity. The purpose of this study is to determine the effectiveness of the BPA cross-linking technique in Saccharomyces cerevisiae by confirming protein-protein interactions between FACT subunits: Spt16 and Pob3. We concluded that the BPA cross-linking technique was effective in confirming the protein-protein interactions between FACT subunits within the dimerization domain.
Probing the Spt16-Pob3 Interface Through BPA Cross-Linking in Saccharomyces cerevisiae as a Proof of Concept
Northwestern College, Rowenhorst Student Center
Examining protein-protein interactions in vivo can often be challenging due to nonspecific cross reactivity. The purpose of this study is to determine the effectiveness of the BPA cross-linking technique in Saccharomyces cerevisiae by confirming protein-protein interactions between FACT subunits: Spt16 and Pob3. We concluded that the BPA cross-linking technique was effective in confirming the protein-protein interactions between FACT subunits within the dimerization domain.