Abstract
This research investigates 24 647 non-homologous protein sequences. The occurrence profile of peptapeptides was constructed for every sequence and hierarchically organized elements of various sizes were revealed by a special mathematical method in each profile. The correlations between these hierarchical elements were analyzed and it was shown that in a tested set of protein sequences there are 11 levels of protein organization with elements ranging in length from 7 to 56 amino acid residues. It was suggested that the identified levels of organization correspond to elements of a super-secondary structure with different topology.
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