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Biophys J, May 1999, p. 2439-2447, Vol. 76, No. 5
*Physics and Pathology, University of British Columbia, Vancouver, British Columbia V6T 1Z1, Canada, and #Biomedical Engineering, Boston University, Boston, Massachusetts 02215 USA
Bond dissociation under steadily rising force occurs most
frequently at a time governed by the rate of loading (Evans and Ritchie, 1997 Biophys. J. 72:1541-1555). Multiplied by the
loading rate, the breakage time specifies the force for most frequent failure (called bond strength) that obeys the same
dependence on loading rate. The spectrum of bond strength versus
log(loading rate) provides an image of the energy landscape traversed
in the course of unbonding. However, when a weak bond is connected to very compliant elements like long polymers, the load applied to the
bond does not rise steadily under constant pulling speed. Because of
nonsteady loading, the most frequent breakage force can differ
significantly from that of a bond loaded at constant rate through stiff
linkages. Using generic models for wormlike and freely jointed chains,
we have analyzed the kinetic process of failure for a bond loaded by
pulling the polymer linkages at constant speed. We find that when
linked by either type of polymer chain, a bond is likely to fail at
lower force under steady separation than through stiff linkages. Quite
unexpectedly, a discontinuous jump can occur in bond strength at slow
separation speed in the case of long polymer linkages. We demonstrate
that the predictions of strength versus log(loading rate) can
rationalize conflicting results obtained recently for unfolding Ig
domains along muscle titin with different force techniques.
Biophys J, May 1999, p. 2439-2447, Vol. 76, No. 5
© 1999 by the Biophysical Society 0006-3495/99/05/2439/09 $2.00
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