Specificity of DNA-basic polypeptide interactions. 11<sup>+</sup>. Influence of aromatic amino acid residues investigated with agarose bound lysine copolypeptides
Wehling, Klaus; Arfmann, Hans-Adolf; Seipke, Gerhard; Wagner, Karl G.; Gesellschaft für Biotechnologische ForschungAbteilung Molekularbiologie, 3300 Braunschweig-Stöckheim, GFR
Журнал:
Nucleic Acids Research
Дата:
1977
Аннотация:
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.
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