Proteomic Code

 Investigation of crystallized protein structures recommends that globular proteins are assembled as consecutively connected units of 25–35 residues. These units are closed loops that are returns of the polypeptide chain orientation to a close contact with itself. The universal characteristic of apparently polymer-statistical nature is a basis for a principally novel view on the globular proteins as loop fold structures. The similar unit size has been discovered in protein chain converted from absolute prokaryotic genomes by positional autocorrelation analysis, which closely specifies the evolutionary connection of the units. The units are further characterized by prototype sequences matching to their several derivatives in the translated genomes. The units belong to a potentially bounded spectrum of the sequence prototypes, full repertoire of which would constitute a proteomic code.