S112: Quantum mechanics and molecular dynamics for design of new enzymes

Quantum mechanics has been used for the location of transition states and positioning of catalytic side chains to stabilize transition states. Proteins that fold to give the required arrangement of side chains for catalysis have been designed and tested for active site stability with molecular dynamics simulations.  In collaboration with David Baker's group and Steven Mayo's group, new catalytic proteins for a variety of reactions have been produced.  Recent advances in this area, including the evaluation of the changes in activity by remote mutations upon directed evolution, will be described.