The ability to specify and design artificial proteins also opens the way for researchers to engineer artificial protein enzymes for use as medicines or industrial catalysts, said the study's lead author, Howard Hughes Medical Institute investigator David Baker at the University of Washington.
Baker and colleagues Brian Kuhlman, who is now at the University of North Carolina, Chapel Hill, and graduate student Gautam Dantas at the University of Washington, published their studies in the November 21, 2003, issue of the journal Science. The scientists collaborated on the studies with other researchers at the University of Washington and the Fred Hutchinson Cancer Research Center in Seattle.
Proteins are initially synthesized as long chains of amino acids and they cannot function properly until they fold into intricate globular structures. Understanding and predicting the rules that govern this complex folding process -- involving the folding of the main backbone and the packing of the molecular side chains of the amino acids -- is one of the central problems of biology.
According to Baker, the ability to specify a desired folded protein structure and then to create that protein offers powerful scientific and practical benefits. "First, specifying a protein fold and then designing that protein is a very stringent test of our current understanding of the forces and energetics of macromolecular systems," he said. "Because designing something that's completely new means you can't copy any aspect from nature.