| Abstract: | Protease-catalyzed peptide synthesis, involving -chymotrypsin as catalyst and unusual amino acids as acyl acceptors, has been studied. The irreversibility of peptide bonds formed by this method has been explained by employing kinetic studies accompanied by computer-aided molecular modelling of the enzyme's active site. Furthermore, the variety of peptides that may be synthesized by this technique has been increased by utilizing unusual amino acids as acyl donors as well as acceptors. Because of the instablity of the native enzyme under the conditions of synthesis, preliminary studies on an alkali-stable Met(O)₁₉₂-chymotrypsin have also been undertaken. |
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