Abstract
Amino-acid sequence studies and crystallographic evidence are used to construct an atomic model of elastase, which is compared with the structure of α-chymotrypsin. The single polypeptide chain of elastase is folded into two distinct and structurally similar halves displaying opposite polarity.
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SHOTTON, D., WATSON, H. Three-dimensional Structure of Tosyl-elastase. Nature 225, 811–816 (1970). https://doi.org/10.1038/225811a0
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DOI: https://doi.org/10.1038/225811a0
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