Beta structures of alternating polypeptides and their possible prebiotic significance

Nature. 1975 Jul 31;256(5516):383-7. doi: 10.1038/256383a0.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Chemical Phenomena
  • Chemistry, Physical
  • Genetic Code
  • Hydrogen-Ion Concentration
  • Lysine
  • Molecular Weight
  • Peptides* / chemical synthesis
  • Protein Conformation
  • Solubility
  • Structure-Activity Relationship
  • Time Factors
  • Valine
  • Viscosity

Substances

  • Peptides
  • Valine
  • Lysine