Dec 1, 1983

Complexes of polyadenylic acid and the methyl esters of amino acids

Origins of Life
M A KhaledJ C Lacey

Abstract

This report includes studies of the binding of the methyl esters of a series of amino acids to polyadenylic acid. The principal data were obtained using proton NMR; however, some additional data were obtained through the study of insoluble complexes and through ultraviolet spectroscopy. The binding constants are in the order Phe greater than Ile greater than or equal to Leu greater than Val greater than Gly, and show a direct correlation with the hydrophobicities of the amino acids. In most cases they are essentially double the binding constants found by Reuben and Polk (1980) for monomeric AMP. All of these amino acids, except Gly, have A as the middle letter of their anticodons, and Phe is the only one with XAA as its only anticodon. It has the anticodon richest in A and has the highest binding constant for A. These results, coupled with other data, continue to support a model of the origin of the code which is based on weak, but selective affinities between amino acids and their anticodons.

  • References13
  • Citations11

References

  • References13
  • Citations11

Citations

Mentioned in this Paper

In Vivo NMR Spectroscopy
Adenine Polynucleotides
Valine
Amino Acids, I.V. solution additive
Complex (molecular entity)
Ultraviolet Spectroscopy
Alloisoleucine
PAPD7 gene
Spectrophotometry, Ultraviolet
Endorphenyl

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