ABSTRACT
Recent interest in the relation of the enzyme structure and functioning has been driven mainly by the prospects for controlled enzyme functioning due to structural modications. In this regard, it is expedient to employ new methods for the analysis of the protein structure: one of the methods is the THz absorption spectroscopy. One of the well-known examples of remarkable modications of enzyme functioning owing to variations in the molecular environment is the inverse functioning of α-chymotrypsin (CT). is enzyme is known to catalyze hydrolysis of peptide bonds in aqueous medium, which is natural environment for many biomolecules (Northrop et al. 1948). However, the enzyme in the nonaqueous medium is involved in dierent reactions, and hence, dierent products can be formed (Ahern and Klibanov 1985; Klibanov 1989). e hydrolytic reactions catalyzed by proteases in water are transformed into transesterication or peptide synthesis in organic media under modied thermodynamic conditions (Ahern and Klibanov 1985; Debulis and Klibanov 1993; Klibanov 1989; Northrop et al. 1948).
