Hsp70-mediated protein refolding in the E-Cell

In this work, we used E-CELL, a software package aiming at large-scale modeling with full object-oriented modeling support, to analyze the 70kDa heat shock protein (Hsp70) chaperone mediated protein folding. We analyzed the kinetic characteristics of this chaperone system during folding of an unfolded protein using computer simulations. Our simulation results are consistent with laboratory experiments reported and support the kinetic partitioning hypothesis. Our model suggests that although the DnaK chaperone system is robust in assisting protein folding, this robustness is limited by the availability of ATP. Based on this model, we also discusse why object-oriented modeling is needed for reducing the complexity in large-scale biochemical models.