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This paper addresses the polar profile of ancient proteins using a comparative study of amino acids found in 25,000,000-year-old shells as described in Abelson's work. We simulated the polar profile with a computer platform that represented an evolutionary computational toy model that mimics the generation of small proteins starting from a pool of amino acid monomers and that included several dynamic properties such as self-replication and fragmentation-recombination of the proteins. The simulations were taken up to 15 generations and produced a considerable number of proteins of 25 amino acids in length. The computational model included the amino acids found in the ancient shells, the thermal degradation factor and the relative abundance of the amino acids observed in the Miller-Urey experimental simulation on prebiotic amino acid formation. We found that the amino acid polar profiles of the ancient shells and those simulated and extrapolated from the Miller-Urey abundances are coincident.