Abstract
It is of great interest and importance to study how different amino acid residues contribute to and affect the properties of proteins coated as films on solid surface. This work shows that the solid/liquid interfacial energy of surface localized amino acid films and their Gibbs energies of transfer at the air/solution interface have the potential to be used as a rapid and simple method for studying the surface properties of proteins. Based on these results, a new polarity scale for amino acids has been proposed. This scale is compared with existing hydropathy scales in a benchmark test using some proteins with solved 3D structure. The proteins were characterized in terms of surface-exposed residues with a computer program, Graphical Representation and Analysis of Surface Properties (GRASP). It was also shown that each amino acid contribution is relative to the total protein surface and the other residues on the surface.
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