Engineering aspartic proteases to probe structure and function relationships.

Recently, protein engineering has been used to interconvert homodimeric and homologous single-chain aspartic proteases, with some success. The independent folding of the domains of these proteases has also permitted the engineering of domain-rearranged protease zymogens and the use of individual domains as probes for structural denaturation. In addition, site-directed mutagenesis has provided insights into the catalytic mechanism and specificity of this family of proteases.