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DTSTART;TZID="Pacific Time (US & Canada)":20261002T161000
DTEND;TZID="Pacific Time (US & Canada)":20261002T170000
SUMMARY:PChem Seminar – Neetika
LOCATION:Fulmer Hall
DESCRIPTION:Speaker: Neetika\n\nGroup: Dr. ChulHee Kang\n\nTitle: Biophysical Characterization of Protein-Protein Interactions Among Sorghum bicolor Flavonoid Biosynthetic Enzymes\n\nAbstract: Sorghum bicolor produces secondary metabolites through the flavonoid and monolignol pathways, which are hypothesized to be organized into dynamic multi-enzyme assemblies (metabolons) that enhance catalytic efficiency through substrate channeling. However, the molecular basis of these enzyme–enzyme interactions remains poorly understood. Here, we integrated structural, biophysical, and biochemical approaches to investigate enzyme interactions in these pathways. X-ray crystallography provided structural models, while Förster resonance energy transfer (FRET) was used to examine their proximity and interaction dynamics. Isothermal titration calorimetry (ITC) quantified binding affinities and thermodynamic contributions, multi-angle light scattering (MALS) characterized the oligomeric states, and activity assays demonstrated increased catalytic activity in the presence of the interacting enzymes. Together, these results support the formation of a dynamic enzyme complex, offering mechanistic insight into metabolon formation.
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