title: Beta structures of alternating polypeptides and their possible prebiotic significance.
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 Beta-sheet structure. Poly(Val-Lys), like other polypeptides in which hydrophobic and hydrophilic residues alternate, tends to form Beta structures. We show that bilayers with a hydrophobic interior and a hydrophilic exterior may be present in aqueous solution.
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005815:Genetic Code; D006863:Hydrogen-Ion Concentration; D008239:Lysine; D008970:Molecular Weight; D010455:Peptides / Q000138:chemical synthesis; D011487:Protein Conformation; D012995:Solubility; D013329:Structure-Activity Relationship; D013997:Time Factors; D014633:Valine; D014783:Viscosity
chemical_list: D010455:Peptides; D014633:Valine; D008239:Lysine