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PMID: 238134 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Beta structures of alternating polypeptides and their possible prebiotic significance.

Nature ·Vol. 256 ·No. 5516 ·1975-07-31 ·Pages 383-7

Brack A, Orgel LE

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
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
Chemicals
Peptides Valine Lysine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Brack A
Orgel L E
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1975-07-31
Pages
383-7
Language
English
Region
England
NLM ID
0410462
Subset
IM
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