• Enhancing the promiscuity of a member of the Caspase protease family by rational design

    2 monthes ago - By Wiley

    Abstract
    The N‐terminal cleavage of fusion tags to restore the native N ‐terminus of recombinant proteins is a challenging task and up to today, protocols need to be optimised for different proteins individually. Within this work, we present a novel protease that was designed in‐silico to yield enhanced promiscuity towards different N ‐terminal amino acids. Two mutations in the active‐site amino acids of human Caspase‐2 were determined to increase the recognition of branched amino‐acids, which show only poor binding capabilities in the unmutated protease. These mutations were determined by...
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