Specificity of DNA basic polypeptide interactions. II+ Influence of aromatic amino acid residues investigated with agarose bound lysine copolypeptides.
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.
D001483:Base Sequence; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D003016:Clostridium perfringens; D004269:DNA, Bacterial / Q000378:metabolism*; D008239:Lysine; D008837:Micrococcus; D010455:Peptides / Q000378:metabolism*; D010649:Phenylalanine; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014364:Tryptophan; D014443:Tyrosine
D004269:DNA, Bacterial; D010455:Peptides; D014443:Tyrosine; D010649:Phenylalanine; D014364:Tryptophan; D008239:Lysine