Abstract
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.
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CITATION STYLE
APA
Craik, D. J. (2012). Turbo-charged crosslinking. Nature Chemistry, 4(8), 600–602. https://doi.org/10.1038/nchem.1417
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