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We show that in experimental atomic force microscopy studies of the lifetimedistribution of mechanically stressed folded proteins the effects of externallyapplied fluctuations can not be distinguished from those of internally presentfluctuations. In certain circumstances this leads to artificiallynon-exponential lifetime distributions which can be misinterpreted as asignature of protein complexity. This work highlights the importance of fullycharacterizing and controlling external sources of fluctuation in mechanicalstudies of proteins before drawing conclusions on the physics at play on themolecular level.

Unfolding protein with an atomic force microscope: Force-fluctuation induced non-exponential kinetics