When: April 12, 2017, 2:00 PM
Location: 3rd Floor Orchard View Room , Discovery Building
Contact: 608-316-4401, email@example.com
High-throughput methods to understand membrane protein oligomerization
Membrane proteins make up a quarter of all genomes and perform an assortment of functions essential to the cell and to the interactions between cells and their environments. Disruptions to their structure can cause a myriad of diseases and thus, membrane proteins are the target of many therapeutics. Despite the biological significance of membrane proteins, there is a lack of knowledge about the forces that govern their folding due to the technical challenges they pose compared to soluble proteins. To explore the biochemical and biophysical properties of membrane proteins, I have focused on the very important subset of membrane proteins that utilize the GASright motif and Cα—H hydrogen bonds. The Senes lab has developed a structural prediction algorithm for the GASright motif, CATM. CATM is based on a minimal set of energy functions (van der Waals and hydrogen bonds) that can predict the structure of GASright motifs to near-atomic precision. Quantitative biophysical techniques are time-consuming and technically challenging, limiting the number of proteins that can be characterized and reduces the chance of discovering general conclusions about the physical properties of the GASright motif. Here, I present an approach that combines high-throughput structural prediction with experimental helix-helix association data. Together, these techniques will produce a structure-based analysis of the forces that drive helix interactions in the context of the GASright motif.
All qBio sponsored talks take place on Wednesdays at 2:00 p.m. in the 3rd floor Orchard View room of the Discovery Building unless otherwise noted. Talks are open to the public. Access to the room is via the elevator behind Aldo’s Cafe in the Northeast corner of the building.