Trends in high pressure bioscience and biotechnology, proceedings vol:19 pages:171-176
International Conference on High Pressure Bioscience and Biotechnology date:2002
Changes in secondary structure of alpha-chymotrypsin were studied in the AOT-water-octane system by Fourier Transform InfraRed spectroscopy in conjunction with pressure. Phase transition in the system, protein structure changes and octane crystallization were observed at different pressure ranges. It was demonstrated that pressure-induced changes in protein structure (formation of partially unfolded states) were responsible for its aggregation when pressure released. This aggregation was accompanied by appearance of special bands (1622 and 1685 cm-1) in the amide I region of the infrared spectra which usually observed upon temperature denaturation. The possibility to regulate the conditions of the formation of protein aggregates is discussed.