Abstract
A set of 24 647 nonhomologous protein sequences was examined. A pentapeptide occurrence profile was constructed for each sequence and hierarchically organized elements of various sizes were detected in each profile by a special mathematical method. Correlations between the hierarchical elements were studied. A total of 11 levels of protein organization with elements ranging from 7 to 56 amino-acid residues were found in the protein sequence set. The organization levels were assumed to correspond to super-secondary structure elements of different topologies.
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