The estimation of affinity constants for the binding of model peptides to DNA by equilibrium dialysis.
The binding of lysine model peptides of the type Lys-X-Lys, Lys-X-X-Lys and Lys-X-X-X-Lys (X = different aliphatic and aromatic amino acids) has been studied by equilibrium dialysis. It was shown that the strong electrostatic binding forces generated by protonated amino groups of lysine can be distinguished from the weak forces stemming from neutral and aromatic spacer amino acids. The overall binding strength of the lysine model peptides is modified by these weak binding forces and the apparent binding constants are influenced more by the hydrophobic character of the spacer amino acid side chains than by the chainlength of the spacers.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004247:DNA; D004269:DNA, Bacterial; D004151:Dipeptides; D007700:Kinetics; D008837:Micrococcus; D008956:Models, Chemical; D009842:Oligopeptides; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013950:Thymus Gland
D004269:DNA, Bacterial; D004151:Dipeptides; D009842:Oligopeptides; D004247:DNA