β structures of alternating polypeptides and their possible prebiotic significance

Details β structures of alternating polypeptides and their possible prebiotic significance β structures of alternating polypeptides and their possible prebiotic significance

Jul 1975

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1975natur.256..383b&link_type=abstract

Nature, Volume 256, Issue 5516, pp. 383-387 (1975).

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21

Scientific paper

A survey of the commonest amino acids formed in prebiotic conditions suggests that the earliest form of genetic coding may have specified polypeptides with a strong tendency to form stable β-sheet structures. Poly(Val-Lys), like other polypeptides in which hydro-phobic and hydrophilic residues alternate, tends to form β structures. We show that bilayers with a hydrophobic interior and a hydrophilic exterior may be present in aqueous solution.

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