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Workshop / Seminar

Eric Jacobo Preliminary Defense

Fulmer Hall
Room 201
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About the event

Speaker:  Eric Jacobo
Group: Dr. Jim Brozik
Location:  Fulmer 201
Time:  9:00-10am

Title:  A Spectroscopic Study of Phenylpropanoid Producing Proteins and Aquaporin-4


Part 1: Sorghum bicolor is a widely grown grain that is used in food, alcohol, livestock feed, and its use to produce biofuels. The phenylpropanoid pathway generates many metabolites that kick off different sub-pathways that produce lignin, flavonoids, and more. The biosynthetic pathway begins with the amino acid phenylalanine, which is converted into p-coumaric acid by three proteins: phenylalanine ammonia-lyase (PAL), cinnamate 4-hydroxylase (C4H), and cytochrome P450 reductase (CPR2). Depending on the plant’s needs, it will take p-coumaric acid and send it through another pathway to produce other primary metabolites, such as flavonoids. The start of flavonoid production begins with a metabolon cluster of chalcone synthase (CHS), chalcone isomerase (CHI), and chalcone isomerase-like protein (CHIL). The thermodynamic driving forces between the plant membrane and protein-protein interactions are unknown. This research aims to use single-molecule fluorescence tracking to measure the thermodynamic driving forces within a plant membrane.

Part 2: Aquaporin-4 (AQP4) is found in the central nervous system (CNS) and is a water channel protein that aids in water homeostasis and neuronal activity. There are two isoforms in the CNS, M1, and M23. The main difference between the two is the length of their N-terminal tail; M1 is longer compared to M23. Due to this discrepancy, M23 can form orthogonal arrays of particles (OAPs) in the plasma membrane. The thermodynamic driving forces that govern self-assembly are still largely unknown. Using one- and two-color single-molecule tracking and super-resolution imaging through collaboration with the Nicchia group from the University of Bari will determine the fundamental thermodynamic driving forces and equilibrium states.