Monday, October 27, 2014

Protein folding: Turbo-charged crosslinking

David J. Craik

The efficient production of stable bioactive proteins often requires the selective formation of several disulfide crosslinks. Two recent studies have now shown that replacing cysteine with selenocysteine in the unfolded protein can autocatalyse the formation of the desired crosslinks.

DOI

Journal: Nature Chemistry

No comments:

Post a Comment