Abstract
The study of mechanical unfolding, through the combined efforts of atomic force microscopy and simulation, is yielding fresh insights into the free-energy landscapes of proteins. One-dimensional models of the free-energy landscape have been widely used to analyze experiments. We show that as the two ends of a protein are pulled apart at a speed tending to zero, the measured mechanical strength of filamin plateaus at about 30 pN instead of going towards zero. Simulations reproduce this phenomenon and indicate that it can be explained by a switch between parallel pathways.
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