Mechanistic basis for ligand-regulated control of protein self-assembly into fibril nano structures

Steve Whitten
Texas State University, San Marcos
Thursday, October 24, 2013
North Carolina State University TBD | 4:30pm

An important property of protein macromolecules is their ability to be controlled by regulatory interactions with cofactors. Using computational tools that simulate protein allosterism, ligand-based control of the self-assembly of alpha-helical folded protein into beta-rich fibril nanostructures was successfully designed into the human prion system. Discussed in this seminar will be: 1) the computational tools that were used to identify regulatory binding sites and design ligand effectors, 2) experimental results demonstrating ligand-control of the fibril conversion, and 3) preliminary results of molecular dynamics simulations performed in collaboration with Yaroslava Yingling's group at NCSU that provide molecular and mechanistic descriptions of the ligand-regulated self-assembly process.