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 C2 and C8 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.
Keywords: PMR spectroscopy, melting temperature, binding constants
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