Abstract
1. 1. Unimolecular films of poly-amino acids at the oil-water interface behave as though the molecules were long, freely flexible chains, in which hydrogen bonds between chains are evidently not maintained. 2. 2. The existing data for proteins at the oil-water surface can be interpreted in the same way. This is supported by the known values of surface viscosity and the recently measured interfacial potentials. At the air-water interface, however, a protein molecule is coiled up due to the action of Van der Waals forces between the non-polar side-chains. 3. 3. Protein molecules at the air-water and oil-water interface are in different degrees of surface denaturation. The corresponding entropies have been calculated.
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