"Our yield is hundredsfold higher compared to the commonly used enzymatic approach," Zhuang says. "We also have the flexibility of modifying the selected residues, which has not been possible with the previous approach."

In investigating the effect of the differently modified proteins, Zhuang and his group also revealed a surprising phenomenon regarding ubiquitylation.

"We found that ubiquitin as a protein modifier is far more flexible than we have thought. This property distinguishes ubiquitylation from other better studied protein post-translational modifications, such as phosphorylation and acetylation," Zhuang says.

The new UD approach will help researchers studying ubiquitin biology by providing the means to prepare milligrams of protein samples for in-depth structural and functional characterization.

Since the publication of the work online in Nature Chemical Biology, Zhuang has received requests for samples from research groups across the United States.

Additionally, the new approach has already opened up doors to new research in Zhuang's own laboratory, where he and his team are investigating new anti-cancer therapies.

Source: University of Delaware