Abstract
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.