This special Physics department colloquium is scheduled for Monday 4/27/15 at 4:00 pm in Room 135. Coffee, tea and cookies are served at 3:45 pm in the same room. Anyone is welcome.

Towards in vivo NMR: Putting prions in context
Dr. Kendra King Frederick, Postdoctoral Scholar, Whitehead Institute, Cambridge, MA

Protein folding and assembly into macromolecular structures happens in crowded environments with the coordinated participation of many biomolecules. Yet, limitations on the specificity and sensitivity of biophysical techniques typically restrict structural investigations to purified systems at concentrations that are orders of magnitude above endogenous levels. I apply a sensitivity-enhancement technique for solid state Nuclear Magnetic Resonance spectroscopy (NMR), dynamic nuclear polarization, to investigate a protein at endogenous concentrations in its native environment. With the goal of understanding how proteins involved in human pathologies such as neurodegenerative diseases interact at both the atomic and molecular levels within cells, work on the yeast prion protein establishes genetic, biochemical and spectroscopic techniques that enable structural and mechanistic investigation of proteins in biologically relevant contexts.