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Force-clamp spectroscopy reveals the unfolding and disulfide bond rupturetimes of single protein molecules as a function of the stretching force, pointmutations and solvent conditions. The statistics of these times reveal whetherthe protein domains are independent of one another, the mechanical hierarchy inthe polyprotein chain, and the functional form of the probability distributionfrom which they originate. It is therefore important to use robust statisticaltests to decipher the correct theoretical model underlying the process. Here wedevelop multiple techniques to compare the well-established experimental dataset on ubiquitin with existing theoretical models as a case study. We show thatrobustness against filtering, agreement with a maximum likelihood function thattakes into account experimental artifacts, the Kuiper statistic test andalignment with synthetic data all identify the Weibull or stretched exponentialdistribution as the best fitting model. Our results are inconsistent withrecently proposed models of Gaussian disorder in the energy landscape or noisein the applied force as explanations for the observed non-exponential kinetics.Since the physical model in the fit affects the characteristic unfolding time,these results have important implications on our understanding of thebiological function of proteins.

Force-clamp analysis techniques reveal stretched exponential unfolding kinetics in ubiquitin