Protein folding

Turbo-charged crosslinking

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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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Figure 1: Illustration of the application of selenocysteine for promoting the oxidative folding of peptides.

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Correspondence to David J. Craik.

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Craik, D. Turbo-charged crosslinking. Nature Chem 4, 600–602 (2012) doi:10.1038/nchem.1417

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