Some proteins keep ``living fossil'' pre-sequence

Details Some proteins keep ``living fossil'' pre-sequence Some proteins keep ``living fossil'' pre-sequence

Apr 1993

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1993oleb...23..115i&link_type=abstract

Origins of Life and Evolution of the Biosphere, Volume 23, Issue 2, pp.115-124

Computer Science

Scientific paper

The sequences of hydrophobic segments of exported bacterial proteins, some serine proteinases and all known plastocyanins are examined in order to find out subsequences differing in amino acid composition and primary structure regularities. It is established that the extension in protein precursor, cleaved by a proteolysis (so-called P-sequence), demonstrates a higher share of usual amino acids (Thr, Pro, Ala, Ser, Arg, Gly, Leu, Val, Glu, Asp) and more clearly expressed periodicity compared to the mature protein (M-sequence). The obtained results confirm the conception of primitive proteins comprising a small number of amino acids realized a preferable bonding (between identical and very similar in structure-function-evolution sense).

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