Updated: Nov 28, 2018
2018 REU Student Profile
Jerrica is currently a student at the Central State University in Wilberforce, Ohio. This summer she is exploring theoretical biochemistry with Professor Stan's research team.
Computational Simulation of Green Fluorescent Protein (GFP) unfolding mediated by 26s Proteasome
In this study, we use a coarse-grained model of AAA+ ATPase motor of 26s proteasome and perform Langevin dynamics simulation of mechanical pulling of GFP through the center pore of AAA ATPase motor. We compare mechanical unfolding of GFP by pulling different directions using constant velocity and repetitive force pulling. 26s Proteasome is an ATP-dependent degradation machine at the center of the ubiquitin-proteasome system and maintains cell viability by unfolding and degradation of ubiquitinated proteins in eukaryotes. 19s regulatory particle (RP) of proteasome contains hetrohexameric AAA+ ATPase motor that unfolds the substrates by threading them into its central pore and then translocate them to the associated peptidase, 20s-CP, for degradation , but the detailed mechanisms of this process remains unknown.