Effect of a cationic surfactant on protein unfolding at the air-solution interface

摘要

Kinetic dependences of the dynamic dilatational surface elasticity of solutions of the complexes of b-lactoglobulin and bovine serum albumin with dodecyltrimethylammonium bromide show that the destruction of the tertiary protein structure and the partial destruction of the secondary structure in the surface layer occur at lower surfactant concentrations than in the bulk solution.