Abstract
Mechanical unfolding of the fourth domain of Distyostelium discoideum filamin (DDFLN4) was studied using a CABS - coarse-grained knowledge-based protein model. Our study demonstrates that CABS is capable of reproducing the unfolding free energy landscape of protein unfolding and highlights an important role of non-native interactions in the protein unfolding process. The obtained three peaks in the force-extension profile suggest a four-state picture of DDFLN4 protein unfolding and correspond reasonably to the results of the all-atom simulation in explicit solvent.
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