The estimation of affinity constants for the binding of model peptides to DNA by equilibrium dialysis.

Nucleic Acids Research
K C Standke, H Brunnert

Abstract

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.

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Citations

Mar 24, 2011·Journal of Agricultural and Food Chemistry·Supaporn NaknukoolMasahiro Ogawa
Sep 1, 1988·Journal of Biochemical and Biophysical Methods·G Desoye
Jan 1, 1981·CRC Critical Reviews in Biochemistry·C Helene, J C Maurizot
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Jan 14, 2012·Journal of Molecular Biology·William A CantaraPaul F Agris
Aug 13, 2003·The Journal of Biological Chemistry·Laurence BrewerRod Balhorn

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