Glassy behavior of intrinsically disordered proteins

Intrinsically disordered proteins keep being a puzzle regarding their behavior and biological function. In this work, we follow the relaxational dynamics of several common intrinsically disordered proteins from 10^-12 to 10^-5 seconds. To this end, we combine extensive Molecular Dynamics simulations (using realistic force fields recently tuned with experiments), with large-scale temperature replica-exchange MD simulations, to access the equilibrium dynamics. We show that the dynamics of intrinsically disordered proteins at room temperatures is far more complex than what previously thought. In particular, they display aging effects, an important dependence of the characteristic times with temperature, and collective relaxations. In summary, their microscopic dynamics resemble very much to that of dense glass forming liquids.