70 years ago, Werner Kuhn and Hans Kuhn proved a theorem asserting that global relaxation of long polymer chains is controlled by hydrodynamic friction alone, with the internal friction effects caused by roughness of their energy landscapes only becoming important for shorter chains. Their ideas are enjoying renewed interest after single-molecule measurements of protein dynamics exposed the utility of polymer physics theories in describing how unfolded proteins explore their energy landscapes while <i>en route</i> to their native state. But what does polymer physics tell us about microscopic details of protein motion? How do proteins behave under the (common) conditions placing them halfway between the internal friction and hydrodynamic friction limits? This talk will describe recent efforts of our group to use coarse grained and atomistic simulations in order to answer these questions and to establish the molecular origins of the phenomenological parameters (such as the internal friction coefficient or the diffusion coefficient along a reaction coordinate) appearing in semi-phenomenological theories of protein dynamics and folding.

Molecular origins of friction in unfolded proteins

251st National Meeting (2016)

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