This group is interested in structural factors that influence and tune reduction potentials in metalloproteins, specifically copper oxidoreductase enzymes. They have determined a series of protein crystal structures of mutants of the small Cu protein azurin, which have varied experimental reduction potentials. The group would like to computationally analyze the environment around the Cu centers in each of these crystal structures, looking for differences such as dipole moments, local charges, solvent content, etc. In collaboration with a colleague, Dr. Alessandro Cembran, they have begun classical molecular dynamics simulations on the crystal structures, using the program GROMACS, to analyze electrostatic differences between mutants. They have also used quantum mechanical means to compute the charges, bonds angles, and distances in the local copper active site. These studies have shed light on potential mechanisms by which reduction potentials are modified in the protein variants. The researchers aim to eventually use higher level QM/MM simulations, using programs such as Gaussian, to describe more of the protein environment.