This energetically favorable position of the agonist makes it possible for additional binding of the ligand to other Ser in the binding site, along with additional anchoring between Phe in the pocket of the binding site and the indole of the agonist.
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Side chains of the surrounding amino acids can have an effect on the binding of the nitrogen atom, mainly three Phe can affect the methyl groups bound to the nitrogen atom (not shown in figure 2).
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The binding of Phe and the triptan is caused by π stacking interactions of the indole and amino acid and an additional effect on this interaction is because of dispersive effect of amino acid leucine (Leu)(not shown in figure 2).
It is associated with a mutation of a phenylalanine to leucine in SEC23A.
The substances are prepared via a Knoevenagel condensation of a thiohydantoin–phenylalanine imine with different aldehydes, which yields a mixture of E and Z isomers.
Whilst a post-doctoral visitor in the laboratory of Marshall Warren Nirenberg at the NIH in Bethesda, Maryland, he discovered that a synthetic RNA polynucleotide, composed of a repeating uridylic acid residue, coded for a polypeptide chain encoding just one kind of amino acid, phenylalanine.
Almost immediately, Marshall Nirenberg and J. Heinrich Matthaei put it to use to form the first three-nucleotide RNA codons, which coded for the amino acid phenylalanine.
In their experiments in late May 1961 they had narrowed down the amino acids encoded by Poly-U to Phenylalanine or Tyrosine.