Abstract
Life on Earth exhibits an amazing adaptive capacity to a vast range of temperatures. While the molecular mechanisms underlying such adaptability are not yet fully understood, it has been proposed that the cell-death temperature coincides with a denaturation catastrophe of the proteome. Here we use multi-scale simulations and neutron scattering experiments to describe the dynamical properties of proteins inside a bacterial cytoplasm when approaching thermal denaturation. Through a combination of extensive coarse-grain and all-atomistic simulations, we characterize distinct contributions to the picosecond- and nanosecond dynamics of proteins immersed in a crowded and heterogeneous environment mimicking the composition of E.
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