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Intrinsically disordered proteins undergo conformational changes that are often beyond the scope of current computational techniques used to study the dynamics of folded proteins. New approaches to define a metric for the dynamics of disordered proteins have been developed which are also readily applicable to the study of non-equilibrium globular protein dynamics. We use dimensionality reduction, dimensionality estimation and clustering techniques applied to molecular dynamics (MD) simulations of a class of entirely disordered proteins (outside of a small anchoring domain) involved in nucleocytoplasmic transport, the FG-nucleoporins (FG-nups), as well as folding simulations of several globular proteins of similar size and sequence composition to compare disordered protein dynamics to early-stage folding dynamics. Our results provide detailed maps of the protein conformation space, allow us to classify proteins based on their dynamics, and indicate that disordered protein motion is of higher-dimensionality than earlystage folding dynamics. Host: Jianhui Tian, T-6: THEORETICAL BIOLOGY AND BIOPHYSICS, tianj@lanl.gov |