Abstract
MANY studies have been made of the specificity of interaction between nucleic acids and polypeptides, proteins and enzymes1,2. Electrostatic forces between basic amino-acids and phosphate groups contribute to the stability of the complexes, but selective recognition requires more specific interactions which are not yet understood. The recognition of a specific region of a nucleic acid could be explained if this region has some particular conformation or if there are specific interactions between a few amino-acid residues and the bases of this region. We wish to report results which show that the aromatic amino-acids tryptophan and tyrosine can interact with nucleic acid bases in double stranded nucleic acids. They suggest that aromatic amino-acid residues of enzymes and proteins could participate in the binding to nucleic acids by intercalating between the bases, and thus constraining the nucleic acid molecule to adopt a definite position with respect to the protein molecule.
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HÉLÈNE, C. Role of Aromatic Amino-acid Residues in the Binding of Enzymes and Proteins to Nucleic Acids. Nature New Biology 234, 120–121 (1971). https://doi.org/10.1038/newbio234120a0
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DOI: https://doi.org/10.1038/newbio234120a0
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