Secondary structure of globular proteins in adsorption layers at the solution-air interface by the data of Fourier transform IR spectroscopy

摘要

The secondary structures of globular proteins of different structural types (alpha, (alpha + beta), and beta) are studied in the adsorption layers at the solution-air interface using Fourier transform infrared spectroscopy. Similar investigations are performed for the initial proteins in a powdered state; these data are used as a control. It is shown that, at the water-air interface, either the secondary structure of the studied proteins changes insignificantly or remains intact depending on the structural type of a protein. The adsorption of proteins of the alpha-helical type (bovine and human serum albumins) and the (alpha + beta) type (lysozyme) virtually do not result in changes in their secondary structure. A protein of beta-structural type, (alpha-chymotrypsin, shows a lower stability at the water-air interface.