Glassy dynamics and memory effects in an intrinsically disordered protein construct

Abstract

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.

6 pages, 3 figures, accepted for publication in Physical Review Letters

References in corpus (1)

• Neurofilaments function as shock absorbers: compression response arising from disordered proteins

Cited by in corpus (1)

• Ubiquitous Dynamical Time Asymmetry in Measurements on Materials and Biological Systems