But the work really began thirty years ago, with basic studies into the structure of proteins. These massive organic molecules contain thousands of atoms that may be configured into many complex forms, as if they were birds or flowers folded from similar sheets of paper.

Proton nuclear magnetic resonance (NMR) has already proven itself for the study of simple molecules, but Oldfield and colleagues have demonstrated that carbon-13 NMR could also be used to study proteins. They showed that experimental NMR spectra of amino acid residues in proteins are predictable with high accuracy by analyzing only small fragments of a protein. Then, using quantum chemistry calculations on the NCSA's SGI Origin2000 cluster, these researchers overturned conventional ideas of how carbon monoxide binds with hemoglobin.