Binding constants of phenylalanine for the four mononucleotides.
Earlier work has shown that several properties of amino acids correlate directly with properties of their anticodonic nucleotides. Furthermore, in precipitation studies with thermal proteinoids and homopolyribonucleotides, an anticodonic preference was displayed between Lys-rich, Pro-rich and Gly-rich thermal proteinoids and their anticodonic polyribonucleotides. However, Phe-rich thermal proteinoid displayed a preference for its codonic nucleotide, poly U. This inconsistency seemed to be explained by a folding in of the hydrophobic residues of Phe causing the proteinoid to appear more hydrophilic. The present work used nuclear magnetic resonance techniques to resolve a limited question: To which of the four nucleotides does Phe bind most strongly? The results show quite clearly that Phe binds most strongly to its anticodonic nucleotide, AMP.
D000249:Adenosine Monophosphate; D000926:Anticodon; D001665:Binding Sites; D005075:Biological Evolution; D005815:Genetic Code; D009682:Magnetic Resonance Spectroscopy; D009711:Nucleotides; D010649:Phenylalanine
D000926:Anticodon; D009711:Nucleotides; D000249:Adenosine Monophosphate; D010649:Phenylalanine