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.
For more information about joining in on Zoom, contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu