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- W3148049158 abstract "1015-Plat Probing the Conformation Landscape of the Unfolded State: Do Disordered and Unfolded Dynamics Differ? Joshua L. Phillips1, Edmond Y. Lau2, Shawn Newsam1, Michael E. Colvin1. University of California, Merced, Merced, CA, USA, Lawrence-Livermore National Laboratory, Livermore, CA, USA. 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 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 (FGnups), 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." @default.
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- W3148049158 date "2011-01-01" @default.
- W3148049158 modified "2023-09-27" @default.
- W3148049158 title "Synaptotagmin Expands Membrane Fusion Pore by Facilitating SNARE-Complex Formation" @default.
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