Figuring out how denatured proteins morph into their folded, active forms isn't just a challenge; it's one of the most elusive problems in biology. Protein chemists now have more computational power to devote to the problem, thanks to a recent award of two million processor hours on the Department of Energy's 10-teraflops IBM supercomputer at the National Energy Research Scientific Computing Center in Berkeley, Calif. The award, part of the Innovative and Novel Computational Impact on Theory and Experiment (INCITE) program, supports a project entitled "Molecular Dynameomics," whose ultimate goal is to create a repository for molecular-dynamics data to be used in protein structure predictions.