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The study investigates the proteolytic degradation of bovine serum albumin (BSA) using Fourier transform infrared (FT-IR) and ultraviolet circular dichroism (UV-CD) spectroscopy to monitor changes in protein conformation. It reveals that proteolysis leads to a decrease in α-helical content and an increase in unordered structures, with a correlation established between the degree of hydrolysis and the concentration of carboxylic groups. The findings demonstrate the effectiveness of both spectroscopic techniq

Author

mohammadgounich

Language

EN