Researchers at the University of Texas at Austin and the University of Michigan have forced an unprecedented evolutionary leap in E. coli bacteria, and findings from their study could have ramifications on protein production for the biotechnology industry.

The development, reported in the Feb. 20 issue of Science, demonstrated how the bacterium created an entirely new way to make disulfide bonds. These bonds compose a protein’s stiffening struts that helps the protein fold into its proper, functional, three-dimensional shape. Improperly folded proteins are implicated in diseases ranging from mad cow disease to Alzheimer’s disease.

Disulfides are also vital for the activity of most proteins injected into people for medical purposes, such as insulin and TPA, a blood clot dissolver injected into people having heart attacks and strokes.