CONFORMATION AND PROPERTIES OF PROTEINS AT LIQUID INTERFACES.

In this bibliography-based review paper the author discussed the following topics - possible effects of interfaces on protein structure; conformation of proteins at the air-water and oil-water interfaces (experiment and theory); rheological properties of films of protein adsorbed at air-water and oil-water interfaces; protein-stabilized disperse systems (colloids, emulsions, foams). It is demonstrated that the degree of surface denaturation and the structure of the resultant adsorbed films at the air-water or oil-water interfaces are dependent upon the native structure and flexibility of the protein molecule. The adsorbed films of proteins can be considered as thin layers of protein gel whose rheological properties are a function of the conformations of the molecules, and crosslinking, within it. Foams are more stable when the adsorbed protein layers have a high dilatational modulus (low compressibility). In contrast, the degree of coalescence in emulsions subjected to large gravitational forces in a centrifuge seems to be more dependent upon the magnitude of the disjoining pressure in the aqueous lamellae between oil droplets.