Hannah Reese.

Graduate Student
University of California, Berkeley

B.S. Chemical Engineering, 2012
North Carolina State University

Office Location: 473A Tan Hall
Office Telephone: 510-643-8340

Previously, research in the Clark lab has detailed a filamentous chaperone, γ-prefoldin, from the thermophilic organism Methanocaldococcus jannaschii. This protein can be dimensionally controlled using a capping protein (Whitehead, 2008) to determine filament length and by truncating the coiled-coil region of the prefoldin unit to determine width (Whitehead, 2009).

My project uses the potential of these filaments to form larger structures and integrate them with motor proteins to investigate the potential of protein nanobots. The F1 portion of Bacillus ps3 ATPase has been quite well studied and characterized. This protein has a natural rotor that can transform chemical energy into mechanical energy, spinning a rotating protein shaft to which additional pieces can be attached. By combining γ-prefoldin’s ability to form controllable structures with the molecular motor, we plan to harness the mechanical energy of ATPase to create a functional, novel, moving protein structure. 
Hobbies: Writing novels and short stories