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β structures of alternating polypeptides and their possible prebiotic significance

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Abstract

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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