Abstract

A new random heteropolymer with mixed hydrophilic and hydrophobic groups coats proteins to help them remain folded and active in environments that would normally unfold and inactivate them (Science 2018, DOI: 10.1126/science.aao0335). Random heteropolymers have been designed before to enhance the properties of small molecules, but not proteins. And researchers have previously enhanced protein stability by incorporating proteins in micelles or sol-gel networks or by combining proteins with polyelectrolytes and other polymers. But the new heteropolymer preserves native protein function and structure more faithfully in both aqueous and organic media, say Ting Xu of the University of California, Berkeley, and coworkers, who developed it. The heteropolymer could have bioremediation applications and allow researchers to make proteins without the help of cells. “This is outstanding work showing the ability of functionally diverse, random copolymers to act as chaperones and protein stabilizers for diverse applica...

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