Inspired by nature

Designed proteins have structural features resembling those of natural active sites Over the past decade, scientists have made exciting progress in designing protein folds entirely on the computer and then successfully synthesizing them in the laboratory ( 1 – 5 ). These designer proteins had the same structure in experiment as in the model and were very stable; however, they lacked important structural features seen in protein interfaces and enzyme active sites. In two reports on pages 680 and 687 of this issue, Boyken et al. ( 6 ) and Jacobs et al. ( 7 ) use the Rosetta biomolecular modeling software to design proteins that include some of these features. Experiments show that these new designs retain high structural precision and stability.