Speaker: Robert B. Best, Senior Investigator Theoretical Biophys. Chem. Section, NIH – NIDDK Bethesda, MD
Title: Structure and dynamics of intrinsically disordered proteins, their complexes and assemblies
Abstract: Intrinsically disordered proteins are now realized to play a variety of important biological roles, yet pose a challenge for experiments, because observed signals are averaged over a very heterogeneous ensemble of structures. Molecular simulations can help to interpret the results, if appropriately parameterized to match experimental data. I will describe our work using both atomistic and coarse-grained simulations to model the structure and dynamics of disordered proteins, and their disordered complexes and assemblies, especially those involving highly charged biomolecules. These include the role of a protein chaperone in the folding of nucleic acids, and the formation of coacervates at lower ionic strength and higher protein concentrations.
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