five

Glassy dynamics and memory effects in an intrinsically disordered protein construct

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http://datadryad.org/dataset/doi%253A10.25349%252FD9RC86
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Glassy, nonexponential relaxations in globular proteins are typically attributed to conformational behaviors that are missing from intrinsically disordered proteins. Yet, we show that single molecules of a disordered-protein construct display two signatures of glassy dynamics, logarithmic relaxations and a Kovacs memory effect, in response to changes in applied tension. We attribute this to the presence of multiple independent local structures in the chain, which we corroborate with a model that correctly predicts the force-dependence of the relaxation. The mechanism established here likely applies to other disordered proteins. Methods The data were collected using a custom-built magnetic tweezer as described in Ribeck et al. (2008) https://doi.org/10.1063/1.2981687. The force on each polymer was determined as described in Lansdorp et al. (2012) https://doi.org/10.1063/1.3687431.
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2021-06-20
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