Interaction of aromatic amino acids with neutral polyadenylic acid.
The aromatic amino acids tryptophan, phenylalanine, and histidine interact with singlestranded polyadenylic acid [poly(A)] as observed by proton magnetic resonance spectroscopy. The chemical shift of the C(2) and C(8) protons of the adenine moiety of poly(A) is consistent with a destacking of the initially partly-stacked polynucleotide chain by the intercalation of the planar ring structure. The relative magnitude of this interaction is tryptophan>phenylalanine>histidine.
D000227:Adenine Nucleotides; D055598:Chemical Phenomena; D002621:Chemistry; D006639:Histidine; D009682:Magnetic Resonance Spectroscopy; D010649:Phenylalanine; D011119:Polynucleotides; D011487:Protein Conformation; D013696:Temperature; D014364:Tryptophan
D000227:Adenine Nucleotides; D011119:Polynucleotides; D010649:Phenylalanine; D006639:Histidine; D014364:Tryptophan