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Nucleic Acids Research, 1977, Vol. 4, No. 3 513-522
© 1977

Articles

Specificity of DNA-basic polypeptide interactions. 11+. Influence of aromatic amino acid residues investigated with agarose bound lysine copolypeptides

Klaus Wehling, Hans-Adolf Arfmann, Gerhard Seipke and Karl G. Wagner

Gesellschaft für Biotechnologische Forschung Abteilung Molekularbiologie, 3300 Braunschweig-Stöckheim, GFR

Received November 8, 1976.

Binding affinities towards DNA and base pair specificities of lysine copolymers, containing different amounts of Phe, Tyr or Trp residues, were estimated using a previously described chromatographic method. Incorporation of few aromatic residues into polylysine causes a decrease in the binding affinity, however, further raising the aromatic residue -lysine ratio results in a continous increase of affinity, which is most pronounced with the Tyr copolymers and not observed with polymers containing neutral aliphatic amino acid residues. AT-specificity increases concomitant with binding affinity in the case of the Tyr copolymers but not with the Phe copolymers. The interaction of DNA with the alternating Phe-Lys polymer is significantly stronger than with the random copolymer of equal residue composition. The molecular and conformational reasons determining specificity are discussed.

+Part I is Ref. 1


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