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The disulfide-bridged chains in the kringle (K) and fibronectin type II (FN2) domains are characterized using a taxonomy that considers the regularities in both β-secondary structure and cystine cluster. The structural core of the kringle fold comprises an assembly of two β-hairpins (a “β-meander”) accommodating two overlapping disulfides; one cystine is incorporated in adjacent β-strands, whereas...
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