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Heterogeneity in biological molecules, resulting in molecule-to-moleculevariations in their dynamics and function, is an emerging theme. To elucidatethe consequences of heterogeneous behavior at the single molecule level, wepropose an exactly solvable model in which the unfolding rate due to mechanicalforce depends parametrically on an auxiliary variable representing an entropybarrier arising from fluctuations in internal dynamics. When the rate offluctuations, a measure of dynamical disorder, is comparable to or smaller thanthe rate of force-induced unbinding, we show that there are two experimentallyobservable consequences: non-exponential survival probability at constantforce, and a heavy-tailed rupture force distribution at constant loading rate.By fitting our analytical expressions to data from single molecule pullingexperiments on proteins and DNA, we quantify the extent of disorder. We showthat only by analyzing data over a wide range of forces and loading rates canthe role of disorder due to internal dynamics be quantitatively assessed.

Evidence of disorder in biological molecules from single molecule pulling experiments