Protein Stability Under Biomolecular Crowding Conditions (2015)

Undergraduates: Zijian Zhou, Austin Smith

Faculty Advisor: Gary Pielak
Department: Chemistry

---

I examined the effect of biomolecular crowding on protein stability. My hypothesis was that non-specific attractive weak interactions of crowding biomolecules would overcome their stabilizing hard-core repulsive forces, and destabilize a model protein, the SH3 domain of the drosophila drk protein (drkN SH3). To test this, I used fluorine nuclear magnetic resonance spectroscopy (NMR) to determine the free energy of opening, i.e. a measurement of protein stability, of drkN under different crowding conditions. Our results showed that crowding inside cells destabilized drkN relative to the stability in dilute solutions.